{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T04:39:55Z","timestamp":1793162395755,"version":"4.5.0"},"reference-count":315,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2019,10,1]],"date-time":"2019-10-01T00:00:00Z","timestamp":1569888000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,10,1]],"date-time":"2019-10-01T00:00:00Z","timestamp":1569888000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,5,17]],"date-time":"2019-05-17T00:00:00Z","timestamp":1558051200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007601","name":"Horizon 2020","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007601","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000865","name":"Bill and Melinda Gates Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000865","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2019,10]]},"DOI":"10.1016\/j.bbagen.2019.05.012","type":"journal-article","created":{"date-parts":[[2019,5,20]],"date-time":"2019-05-20T01:47:21Z","timestamp":1558316841000},"page":"1480-1497","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":500,"title":["Exploitation of glycosylation in enveloped virus pathobiology"],"prefix":"10.1016","volume":"1863","author":[{"given":"Yasunori","family":"Watanabe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas A.","family":"Bowden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian A.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Max","family":"Crispin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2019.05.012_bb0005","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1038\/nature06536","article-title":"Global trends in emerging infectious diseases","volume":"451","author":"Jones","year":"2008","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0010","doi-asserted-by":"crossref","first-page":"3693","DOI":"10.1038\/s41467-018-06121-4","article-title":"Differential processing of HIV envelope glycans on the virus and soluble recombinant trimer","volume":"9","author":"Cao","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0015","doi-asserted-by":"crossref","first-page":"1958","DOI":"10.1016\/j.celrep.2018.07.080","article-title":"Site-specific glycosylation of virion-derived HIV-1 Env Is mimicked by a soluble trimeric immunogen","volume":"24","author":"Struwe","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0020","doi-asserted-by":"crossref","first-page":"32956","DOI":"10.1038\/srep32956","article-title":"Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding","volume":"6","author":"Panico","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0025","doi-asserted-by":"crossref","first-page":"3446","DOI":"10.1128\/JVI.06147-11","article-title":"Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin","volume":"86","author":"Kobayashi","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0030","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1164\/rccm.201007-1184OC","article-title":"Glycan shielding of the Influenza virus hemagglutinin contributes to immunopathology in mice","volume":"183","author":"Wanzeck","year":"2011","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0035","doi-asserted-by":"crossref","first-page":"3614","DOI":"10.1038\/ncomms4614","article-title":"Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus","volume":"5","author":"Lee","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0040","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nsmb.3293","article-title":"Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy","volume":"23","author":"Walls","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0045","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01628-17","article-title":"Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections","volume":"92","author":"Xiong","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0050","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.virol.2009.12.020","article-title":"Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein","volume":"399","author":"Ritchie","year":"2010","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0055","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1002\/rcm.4410","article-title":"Identification of N-glycans from Ebola virus glycoproteins by matrix-assisted laser desorption\/ionisation time-of-flight and negative ion electrospray tandem mass spectrometry","volume":"24","author":"Ritchie","year":"2010","journal-title":"Rapid Commun. Mass Spectrom."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0060","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nature07082","article-title":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor","volume":"454","author":"Lee","year":"2008","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0065","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005276","article-title":"Arenavirus glycan shield promotes neutralizing antibody evasion and protracted infection","volume":"11","author":"Sommerstein","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0070","doi-asserted-by":"crossref","first-page":"7136","DOI":"10.1128\/JVI.00116-07","article-title":"Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation","volume":"81","author":"Mondotte","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0075","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1016\/j.celrep.2017.10.016","article-title":"Functional analysis of glycosylation of Zika virus envelope protein","volume":"21","author":"Fontes-Garfias","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0080","doi-asserted-by":"crossref","first-page":"6104","DOI":"10.1128\/JVI.73.7.6104-6110.1999","article-title":"Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion","volume":"73","author":"Flamand","year":"1999","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0085","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003065","article-title":"Antigenic subversion: a novel mechanism of host immune evasion by Ebola virus","volume":"8","author":"Mohan","year":"2012","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0090","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1128\/CVI.00051-06","article-title":"Mature glycoprotein G Presents high performance in diagnosing Herpes Simplex Virus type 2 infection in sera of different Tanzanian cohorts","volume":"13","author":"Gorander","year":"2006","journal-title":"Clin. Vaccine Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0095","series-title":"Introduction to Glycobiology","author":"Taylor","year":"2011"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0100","series-title":"Biological Functions of Glycans","author":"Varki","year":"2015"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0105","doi-asserted-by":"crossref","first-page":"43R","DOI":"10.1093\/glycob\/12.4.43R","article-title":"Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds","volume":"12","author":"Spiro","year":"2002","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0110","series-title":"Essentials of Glycobiology","author":"Varki","year":"2009"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0115","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1093\/bmb\/58.1.19","article-title":"Evolutionary and immunological implications of contemporary HIV-1 variation","volume":"58","author":"Korber","year":"2001","journal-title":"Br. Med. Bull."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0120","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1128\/jvi.71.2.1162-1172.1997","article-title":"Immunocytochemical analysis of Uukuniemi virus budding compartments: role of the intermediate compartment and the Golgi stack in virus maturation","volume":"71","author":"J\u00e4ntti","year":"1997","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0125","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.virol.2006.11.027","article-title":"The intracellular sites of early replication and budding of SARS-coronavirus","volume":"361","author":"Stertz","year":"2007","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0130","doi-asserted-by":"crossref","first-page":"10558","DOI":"10.1128\/JVI.01615-16","article-title":"Hepatitis C Virus is released via a noncanonical secretory route","volume":"90","author":"Bayer","year":"2016","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0135","doi-asserted-by":"crossref","first-page":"13800","DOI":"10.1073\/pnas.1006498107","article-title":"Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens","volume":"107","author":"Doores","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0140","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0023521","article-title":"The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade","volume":"6","author":"Bonomelli","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0145","doi-asserted-by":"crossref","first-page":"8932","DOI":"10.1128\/JVI.01190-15","article-title":"Cell- and protein-directed glycosylation of native cleaved HIV-1 envelope","volume":"89","author":"Pritchard","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0150","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1006\/viro.1997.8453","article-title":"Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations","volume":"230","author":"Gluschankof","year":"1997","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0155","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1002\/pmic.200900096","article-title":"Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds","volume":"9","author":"Harvey","year":"2009","journal-title":"Proteomics."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0160","doi-asserted-by":"crossref","first-page":"11848","DOI":"10.1073\/pnas.1102664108","article-title":"Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein\/amyloid beta-peptides in human cerebrospinal fluid","volume":"108","author":"Halim","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0165","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1038\/emboj.2013.79","article-title":"Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology","volume":"32","author":"Steentoft","year":"2013","journal-title":"EMBO J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0170","doi-asserted-by":"crossref","first-page":"4991","DOI":"10.3390\/ijms11124991","article-title":"Computational prediction of O-linked glycosylation sites that preferentially map on intrinsically disordered regions of extracellular proteins","volume":"11","author":"Nishikawa","year":"2010","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0175","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004784","article-title":"A strategy for O-glycoproteomics of enveloped viruses\u2014the O-glycoproteome of Herpes Simplex virus type 1","volume":"11","author":"Bagdonaite","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0180","doi-asserted-by":"crossref","first-page":"12014","DOI":"10.1074\/jbc.M116.721746","article-title":"Global mapping of O-glycosylation of Varicella Zoster virus, human Cytomegalovirus, and Epstein-Barr virus","volume":"291","author":"Bagdonaite","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0185","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/ni.3319","article-title":"An innate antiviral pathway acting before interferons at epithelial surfaces","volume":"17","author":"Iversen","year":"2016","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0190","doi-asserted-by":"crossref","first-page":"S825","DOI":"10.1093\/infdis\/jir295","article-title":"Impact of Ebola mucin-like domain on antiglycoprotein antibody responses induced by Ebola virus-like particles","volume":"204","author":"Martinez","year":"2011","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0195","doi-asserted-by":"crossref","first-page":"5078","DOI":"10.1074\/jbc.M114.616409","article-title":"O-Linked glycosylation of the mucin domain of the Herpes Simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner","volume":"290","author":"Nord\u00e9n","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0200","first-page":"83","article-title":"Structure and function of respiratory syncytial virus surface glycoproteins","volume":"372","author":"McLellan","year":"2013","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0205","doi-asserted-by":"crossref","first-page":"43701","DOI":"10.1074\/jbc.M111.309096","article-title":"Mimivirus collagen is modified by bifunctional lysyl hydroxylase and glycosyltransferase enzyme","volume":"286","author":"Luther","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0210","doi-asserted-by":"crossref","first-page":"12265","DOI":"10.1128\/JVI.01303-10","article-title":"Crystal structure of a virus-encoded putative glycosyltransferase","volume":"84","author":"Xiang","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0215","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.1099\/vir.0.80320-0","article-title":"Glycosyltransferases encoded by viruses","volume":"85","author":"Markine-Goriaynoff","year":"2004","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0220","doi-asserted-by":"crossref","first-page":"7385","DOI":"10.1074\/jbc.M117.783217","article-title":"The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers","volume":"292","author":"Piacente","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0225","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1080\/14789450.2018.1404907","article-title":"The sweet spot for biologics: recent advances in characterization of biotherapeutic glycoproteins","volume":"15","author":"O'Flaherty","year":"2018","journal-title":"Expert Rev. Proteomics."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0230","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1016\/j.bbapap.2014.05.002","article-title":"Advances in LC\u2013MS\/MS-based glycoproteomics: Getting closer to system-wide site-specific mapping of the N- and O-glycoproteome","volume":"1844","author":"Thaysen-Andersen","year":"2014","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0235","doi-asserted-by":"crossref","DOI":"10.1002\/mas.21586","article-title":"Global and site-specific analysis of protein glycosylation in complex biological systems with mass spectrometry","author":"Xiao","year":"2019","journal-title":"Mass Spectrom. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0240","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S0076-6879(10)80033-3","article-title":"Use of glycan microarrays to explore specificity of glycan-binding proteins","volume":"480","author":"Smith","year":"2010","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0245","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1146\/annurev-biochem-061809-152236","article-title":"Glycan microarrays for decoding the glycome","volume":"80","author":"Rillahan","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0250","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1093\/glycob\/cwh106","article-title":"Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin","volume":"14","author":"Zhang","year":"2004","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0255","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/j.celrep.2018.09.087","article-title":"Completeness of HIV-1 envelope glycan shield at transmission determines neutralization breadth","volume":"25","author":"Wagh","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0260","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1021\/pr401162k","article-title":"Structural plasticity of the Semliki Forest Virus glycome upon interspecies transmission","volume":"13","author":"Crispin","year":"2014","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0265","doi-asserted-by":"crossref","first-page":"1875","DOI":"10.1128\/JVI.01822-10","article-title":"Receptor binding profiles of avian influenza virus hemagglutinin subtypes on human cells as a predictor of pandemic potential","volume":"85","author":"Shelton","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0270","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev.bi.54.070185.003215","article-title":"Assembly of asparagine-linked oligosaccharides","volume":"54","author":"Kornfeld","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0275","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1111\/j.1399-3089.2007.00377.x","article-title":"Natural protection from zoonosis by alpha-gal epitopes on virus particles in xenotransmission","volume":"14","author":"Kim","year":"2007","journal-title":"Xenotransplantation."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0280","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.1042\/BST0391334","article-title":"Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses","volume":"39","author":"Antonopoulos","year":"2011","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0285","first-page":"1140","article-title":"Natural anti-carbohydrate antibodies contributing to evolutionary survival of primates in viral epidemics?","volume":"26","author":"Galili","year":"2016","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0290","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/S0304-4165(99)00170-1","article-title":"Pathways of O-glycan biosynthesis in cancer cells","volume":"1473","author":"Brockhausen","year":"1999","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0295","doi-asserted-by":"crossref","first-page":"4693","DOI":"10.1182\/blood-2004-11-4267","article-title":"HIV-1 incorporates ABO histo-blood group antigens that sensitize virions to complement-mediated inactivation","volume":"105","author":"Neil","year":"2005","journal-title":"Blood."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0300","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1128\/CMR.00109-14","article-title":"Blood groups in infection and host susceptibility","volume":"28","author":"Cooling","year":"2015","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0305","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1098\/rspb.2004.2674","article-title":"Evolution of the human ABO polymorphism by two complementary selective pressures","volume":"271","author":"Seymour","year":"2004","journal-title":"Proc. Biol. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0310","doi-asserted-by":"crossref","first-page":"8502","DOI":"10.1128\/JVI.74.18.8502-8512.2000","article-title":"Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals","volume":"74","author":"Matrosovich","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0315","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1038\/440435a","article-title":"Influenza virus receptors in the human airway","volume":"440","author":"Shinya","year":"2006","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0320","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1186\/1465-9921-8-73","article-title":"Sialic acid receptor detection in the human respiratory tract: evidence for widespread distribution of potential binding sites for human and avian influenza viruses","volume":"8","author":"Nicholls","year":"2007","journal-title":"Respir. Res."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0325","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1750-2659.2008.00051.x","article-title":"Sialic acid tissue distribution and influenza virus tropism","volume":"2","author":"Kumlin","year":"2008","journal-title":"Influenza Other Respir. Viruses"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0330","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.2174\/138945007782151360","article-title":"Protein N-glycosylation in the baculovirus-insect cell system","volume":"8","author":"Shi","year":"2007","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0335","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.febslet.2004.04.045","article-title":"Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure","volume":"566","author":"Max Crispin","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0340","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.mam.2016.04.004","article-title":"Emerging roles of protein mannosylation in inflammation and infection","volume":"51","author":"Loke","year":"2016","journal-title":"Mol. Asp. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0345","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1038\/nchembio.1651","article-title":"The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis","volume":"10","author":"Hebert","year":"2014","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0350","doi-asserted-by":"crossref","first-page":"R155","DOI":"10.1016\/S0969-2126(99)80095-1","article-title":"Glycoproteins: glycan presentation and protein-fold stability","volume":"7","author":"Wormald","year":"1999","journal-title":"Structure."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0355","doi-asserted-by":"crossref","first-page":"13725","DOI":"10.1128\/JVI.79.21.13725-13734.2005","article-title":"Role of N-linked glycans on bunyamwera virus glycoproteins in intracellular trafficking, protein folding, and virus infectivity","volume":"79","author":"Shi","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0360","doi-asserted-by":"crossref","first-page":"5414","DOI":"10.1128\/JVI.78.10.5414-5422.2004","article-title":"Analysis of N-linked glycosylation of hantaan virus glycoproteins and the role of oligosaccharide side chains in protein folding and intracellular trafficking","volume":"78","author":"Shi","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0365","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1099\/jgv.0.000404","article-title":"Mutational and functional analysis of N-linked glycosylation of envelope fusion protein F of Helicoverpa armigera nucleopolyhedrovirus","volume":"97","author":"Li","year":"2016","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0370","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1006\/viro.1997.8570","article-title":"Changes in the Dengue virus major envelope protein on passaging and their localization on the three-dimensional structure of the protein","volume":"232","author":"Lee","year":"1997","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0375","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1006\/viro.1993.1252","article-title":"Selection and partial characterization of Dengue 2 virus mutants that induce fusion at elevated pH","volume":"194","author":"Guirakhoo","year":"1993","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0380","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1099\/0022-1317-80-4-887","article-title":"Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complex","volume":"80","author":"Dubuisson","year":"1999","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0385","doi-asserted-by":"crossref","first-page":"7274","DOI":"10.1128\/JVI.78.13.7274-7278.2004","article-title":"Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein","volume":"78","author":"Moll","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0390","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.virol.2015.04.005","article-title":"Contribution of N-linked glycans on HSV-2 gB to cell\u2013cell fusion and viral entry","volume":"483","author":"Luo","year":"2015","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0395","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/1742-4690-10-14","article-title":"A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization","volume":"10","author":"Wang","year":"2013","journal-title":"Retrovirology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0400","doi-asserted-by":"crossref","first-page":"42900","DOI":"10.1074\/jbc.M111.274456","article-title":"The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry","volume":"286","author":"Fran\u00e7ois","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0405","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1002\/prot.24747","article-title":"Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262","volume":"83","author":"Kong","year":"2015","journal-title":"Proteins."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0410","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1099\/vir.0.000082","article-title":"Role of stem glycans attached to haemagglutinin in the biological characteristics of H5N1 avian influenza virus","volume":"96","author":"Wang","year":"2015","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0415","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/330074a0","article-title":"Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase","volume":"330","author":"Gruters","year":"1987","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0420","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/0014-5793(88)80185-6","article-title":"Inhibition of HIV replication by amino-sugar derivatives","volume":"237","author":"Fleet","year":"1988","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0425","first-page":"139","article-title":"The safety and efficacy of combination N-butyl-deoxynojirimycin (SC-48334) and zidovudine in patients with HIV-1 infection and 200-500 CD4 cells\/mm3","volume":"7","author":"Fischl","year":"1994","journal-title":"J. Acquir. Immune Defic. Syndr."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0430","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1093\/jac\/dku349","article-title":"Strain-specific antiviral activity of iminosugars against human influenza A viruses","volume":"70","author":"Hussain","year":"2015","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0435","doi-asserted-by":"crossref","first-page":"6787","DOI":"10.1073\/pnas.79.22.6787","article-title":"Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol","volume":"79","author":"Datema","year":"1982","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0440","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0167018","article-title":"Minimal in vivo efficacy of iminosugars in a lethal Ebola virus guinea pig model","volume":"11","author":"Miller","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0445","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.antiviral.2013.03.023","article-title":"Small molecule inhibitors of ER \u03b1-glucosidases are active against multiple hemorrhagic fever viruses","volume":"98","author":"Chang","year":"2013","journal-title":"Antivir. Res."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0450","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0004524","article-title":"Iminosugars inhibit Dengue virus production via inhibition of ER alpha-glucosidases\u2014not glycolipid processing enzymes","volume":"10","author":"Sayce","year":"2016","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0455","doi-asserted-by":"crossref","first-page":"6379","DOI":"10.1128\/AAC.01554-12","article-title":"Liposome-mediated delivery of iminosugars enhances efficacy against dengue virus in vivo","volume":"56","author":"Miller","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0460","doi-asserted-by":"crossref","first-page":"3596","DOI":"10.1128\/JVI.76.8.3596-3604.2002","article-title":"Antiviral effects of an iminosugar derivative on flavivirus infections","volume":"76","author":"Wu","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0465","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1042\/BST20160182","article-title":"Iminosugar antivirals: the therapeutic sweet spot","volume":"45","author":"Alonzi","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0470","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1021\/acschembio.7b00870","article-title":"ToP-DNJ, a selective inhibitor of endoplasmic reticulum \u03b1-glucosidase II exhibiting antiflaviviral activity","volume":"13","author":"Kiappes","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0475","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1093\/glycob\/cwy021","article-title":"Global aspects of viral glycosylation","volume":"28","author":"Bagdonaite","year":"2018","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0480","doi-asserted-by":"crossref","first-page":"26","DOI":"10.32607\/20758251-2009-1-2-26-32","article-title":"Influenza virus neuraminidase: structure and function","volume":"1","author":"Shtyrya","year":"2009","journal-title":"Acta Nat."},{"issue":"Suppl. 4","key":"10.1016\/j.bbagen.2019.05.012_bb0485","doi-asserted-by":"crossref","first-page":"D49","DOI":"10.1016\/j.vaccine.2008.07.039","article-title":"The biology of influenza viruses","volume":"26","author":"Bouvier","year":"2008","journal-title":"Vaccine."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0490","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1099\/0022-1317-33-1-159","article-title":"Inhibition of Influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action","volume":"33","author":"Palese","year":"1976","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0495","doi-asserted-by":"crossref","first-page":"12665","DOI":"10.1128\/JVI.78.22.12665-12667.2004","article-title":"Neuraminidase is important for the initiation of Influenza virus infection in human airway epithelium","volume":"78","author":"Matrosovich","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0500","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1128\/jvi.59.2.392-400.1986","article-title":"Intracellular maturation of mumps virus hemagglutinin-neuraminidase glycoprotein: conformational changes detected with monoclonal antibodies","volume":"59","author":"Waxham","year":"1986","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0505","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00803-13","article-title":"Interaction between the Hemagglutinin-Neuraminidase and Fusion glycoproteins of Human Parainfluenza virus type III regulates viral growth in vivo","volume":"4","author":"Xu","year":"2013","journal-title":"MBio."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0510","doi-asserted-by":"crossref","first-page":"1816","DOI":"10.1128\/JVI.76.4.1816-1824.2002","article-title":"Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion","volume":"76","author":"Connaris","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0515","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005390","article-title":"Emerging Paramyxoviruses: receptor tropism and zoonotic potential","volume":"12","author":"Zeltina","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0520","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1038\/nrd2400","article-title":"The war against influenza: discovery and development of sialidase inhibitors","volume":"6","author":"von Itzstein","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0525","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1038\/81002","article-title":"Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase","volume":"7","author":"Taylor","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0530","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.cell.2018.03.030","article-title":"Influenza infection in humans induces broadly cross-reactive and protective neuraminidase-reactive antibodies","volume":"173","author":"Chen","year":"2018","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0535","doi-asserted-by":"crossref","DOI":"10.1093\/infdis\/jiz010","article-title":"Antibody determinants of influenza immunity","author":"Crowe","year":"2019","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0540","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0196771","article-title":"Anti-neuraminidase antibodies against pandemic A\/H1N1 influenza viruses in healthy and influenza-infected individuals","volume":"13","author":"Desheva","year":"2018","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0545","doi-asserted-by":"crossref","first-page":"6739","DOI":"10.3390\/v7122969","article-title":"Ebola virus infections in nonhuman primates are temporally influenced by glycoprotein poly-U editing site populations in the exposure material","volume":"7","author":"Trefry","year":"2015","journal-title":"Viruses."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0550","doi-asserted-by":"crossref","first-page":"S235","DOI":"10.1086\/514280","article-title":"Recombinant human monoclonal antibodies to Ebola virus","volume":"179","author":"Maruyama","year":"1999","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0555","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1007\/s00251-005-0047-4","article-title":"Analysis of the expressed heavy chain variable-region genes of Macaca fascicularis and isolation of monoclonal antibodies specific for the Ebola virus\u2019 soluble glycoprotein","volume":"57","author":"Druar","year":"2005","journal-title":"Immunogenetics."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0560","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003258","article-title":"The secret life of viral entry glycoproteins: moonlighting in immune evasion","volume":"9","author":"Cook","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0565","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2018.07.033","article-title":"Viral Hemorrhagic Fever Immunotherapeutic Consortium, Systematic analysis of monoclonal antibodies against Ebola virus GP defines features that contribute to protection","volume":"174","author":"Saphire","year":"2018","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0570","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1186\/1743-422X-6-147","article-title":"Characterization of the Lassa virus GP1 ectodomain shedding: implications for improved diagnostic platforms","volume":"6","author":"Branco","year":"2009","journal-title":"Virol. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0575","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1186\/1743-422X-7-306","article-title":"Shedding of soluble glycoprotein 1 detected during acute Lassa virus infection in human subjects","volume":"7","author":"Branco","year":"2010","journal-title":"Virol. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0580","doi-asserted-by":"crossref","first-page":"7584","DOI":"10.1128\/JVI.00651-15","article-title":"Molecular mechanism for LAMP1 recognition by Lassa virus","volume":"89","author":"Cohen-Dvashi","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0585","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1126\/science.aam7260","article-title":"Structural basis for antibody-mediated neutralization of Lassa virus","volume":"356","author":"Hastie","year":"2017","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0590","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01048-18","article-title":"Structure-based classification defines the discrete conformational classes adopted by the arenaviral GP1","volume":"93","author":"Pryce","year":"2019","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0595","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1006337","article-title":"Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses","volume":"13","author":"Israeli","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0600","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.virol.2011.02.022","article-title":"N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement","volume":"413","author":"Somnuke","year":"2011","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0605","doi-asserted-by":"crossref","first-page":"e183","DOI":"10.1371\/journal.ppat.0030183","article-title":"Secreted NS1 of Dengue virus attaches to the surface of cells via interactions with heparan sulfate and chondroitin sulfate","volume":"3","author":"Avirutnan","year":"2007","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0610","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005277","article-title":"Dengue virus non-structural protein 1 modulates infectious particle production via interaction with the structural proteins","volume":"11","author":"Scaturro","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0615","doi-asserted-by":"crossref","first-page":"424","DOI":"10.4049\/jimmunol.1100750","article-title":"Binding of Flavivirus nonstructural protein NS1 to C4b binding protein modulates complement activation","volume":"187","author":"Avirutnan","year":"2011","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0620","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.4049\/jimmunol.1600323","article-title":"Secreted NS1 protects Dengue virus from mannose-binding lectin\u2013mediated neutralization","volume":"197","author":"Thiemmeca","year":"2016","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0625","doi-asserted-by":"crossref","first-page":"304ra141","DOI":"10.1126\/scitranslmed.aaa3787","article-title":"Dengue virus NS1 triggers endothelial permeability and vascular leak that is prevented by NS1 vaccination","volume":"7","author":"Beatty","year":"2015","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0630","doi-asserted-by":"crossref","first-page":"12191","DOI":"10.1128\/JVI.01604-08","article-title":"The secreted form of Respiratory Syncytial Virus G glycoprotein helps the virus evade antibody-mediated restriction of replication by acting as an antigen decoy and through effects on Fc receptor-bearing leukocytes","volume":"82","author":"Bukreyev","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0635","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1128\/JVI.79.2.841-852.2005","article-title":"Epstein-Barr Virus gp42 Is posttranslationally modified to produce soluble gp42 that mediates HLA class II immune evasion","volume":"79","author":"Ressing","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0640","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1089\/vim.2012.0034","article-title":"Epstein-Barr virus-encoded BARF1 protein is a decoy receptor for macrophage colony stimulating factor and interferes with macrophage differentiation and activation","volume":"25","author":"Hoebe","year":"2012","journal-title":"Viral Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0645","doi-asserted-by":"crossref","first-page":"2515","DOI":"10.1128\/JVI.80.5.2515-2528.2006","article-title":"Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1","volume":"80","author":"Moore","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0650","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1084\/jem.182.1.185","article-title":"Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer","volume":"182","author":"Sattentau","year":"1995","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0655","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003618","article-title":"A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies","volume":"9","author":"Sanders","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0660","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1016\/j.cell.2015.11.056","article-title":"Immunogenicity of stabilized HIV-1 envelope trimers with reduced exposure of non-neutralizing epitopes","volume":"163","author":"de Taeye","year":"2015","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0665","doi-asserted-by":"crossref","first-page":"11905","DOI":"10.1128\/JVI.01548-10","article-title":"Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions","volume":"84","author":"Helle","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0670","doi-asserted-by":"crossref","first-page":"910","DOI":"10.3389\/fimmu.2018.00910","article-title":"Glycan shielding and modulation of Hepatitis C virus neutralizing antibodies","volume":"9","author":"Lavie","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0675","doi-asserted-by":"crossref","first-page":"9049","DOI":"10.1128\/JVI.01161-14","article-title":"Modification of the hepatitis B virus envelope protein glycosylation pattern interferes with secretion of viral particles, infectivity, and susceptibility to neutralizing antibodies","volume":"88","author":"Julithe","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0680","doi-asserted-by":"crossref","first-page":"7235","DOI":"10.1128\/JVI.00773-15","article-title":"Novel functions of Hendra virus G N-glycans and comparisons to Nipah virus","volume":"89","author":"Bradel-Tretheway","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0685","doi-asserted-by":"crossref","first-page":"2501","DOI":"10.1128\/JVI.06380-11","article-title":"Coordinate deletion of N-glycans from the heptad repeats of the fusion F protein of Newcastle disease virus yields a hyperfusogenic virus with increased replication, virulence, and immunogenicity","volume":"86","author":"Samal","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0690","doi-asserted-by":"crossref","first-page":"5184","DOI":"10.1128\/jvi.63.12.5184-5193.1989","article-title":"Influence of asparagine-linked oligosaccharides on antigenicity, processing, and cell surface expression of herpes simplex virus type 1 glycoprotein D","volume":"63","author":"Sodora","year":"1989","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0695","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002387","article-title":"Antibody evasion by a gammaherpesvirus O-glycan shield","volume":"7","author":"Machiels","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0700","doi-asserted-by":"crossref","first-page":"7320","DOI":"10.1073\/pnas.1803990115","article-title":"Structure of the Lassa virus glycan shield provides a model for immunological resistance","volume":"115","author":"Watanabe","year":"2018","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0705","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/nature18615","article-title":"Toremifene interacts with and destabilizes the Ebola virus glycoprotein","volume":"535","author":"Zhao","year":"2016","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0710","doi-asserted-by":"crossref","first-page":"3614","DOI":"10.1038\/ncomms4614","article-title":"Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus","volume":"5","author":"Lee","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0715","doi-asserted-by":"crossref","first-page":"3957","DOI":"10.1021\/acs.jproteome.5b00416","article-title":"Glycosylation analysis of engineered H3N2 Influenza A virus hemagglutinins with sequentially added historically relevant glycosylation sites","volume":"14","author":"An","year":"2015","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0720","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/nsmb.3051","article-title":"Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env","volume":"22","author":"Do Kwon","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0725","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005322","article-title":"Crystal structure of the pre-fusion Nipah virus fusion glycoprotein reveals a novel hexamer-of-trimers assembly","volume":"11","author":"Xu","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0730","doi-asserted-by":"crossref","DOI":"10.1146\/annurev-biophys-060414-034156","article-title":"Structure and immune recognition of the HIV glycan shield","volume":"47","author":"Crispin","year":"2018","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0735","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1038\/360358a0","article-title":"Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60","volume":"360","author":"Hallenberger","year":"1992","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0740","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.34271","article-title":"HIV-1 Env trimer opens through an asymmetric intermediate in which individual protomers adopt distinct conformations","volume":"7","author":"Ma","year":"2018","journal-title":"Elife."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0745","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1111\/imr.12507","article-title":"The HIV-1 envelope glycoprotein structure: nailing down a moving target","volume":"275","author":"Ward","year":"2017","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0750","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1038\/31514","article-title":"The antigenic structure of the HIV gp120 envelope glycoprotein","volume":"393","author":"Wyatt","year":"1998","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0755","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nature01470","article-title":"Antibody neutralization and escape by HIV-1","volume":"422","author":"Wei","year":"2003","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0760","doi-asserted-by":"crossref","first-page":"7479","DOI":"10.1038\/ncomms8479","article-title":"Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies","volume":"6","author":"Pritchard","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0765","doi-asserted-by":"crossref","first-page":"2695","DOI":"10.1016\/j.celrep.2016.02.058","article-title":"Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein","volume":"14","author":"Behrens","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0770","doi-asserted-by":"crossref","first-page":"14954","DOI":"10.1038\/ncomms14954","article-title":"Global site-specific N-glycosylation analysis of HIV envelope glycoprotein","volume":"8","author":"Cao","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0775","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01894-16","article-title":"Molecular architecture of the cleavage-dependent mannose patch on a soluble HIV-1 envelope glycoprotein trimer","volume":"91","author":"Behrens","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0780","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1016\/j.celrep.2015.05.017","article-title":"Structural constraints determine the glycosylation of HIV-1 envelope trimers","volume":"11","author":"Pritchard","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0785","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.sbi.2017.03.008","article-title":"Structural principles controlling HIV envelope glycosylation","volume":"44","author":"Behrens","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0790","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.coviro.2015.02.002","article-title":"Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design","volume":"11","author":"Crispin","year":"2015","journal-title":"Curr. Opin. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0795","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1146\/annurev-immunol-041015-055515","article-title":"Broadly neutralizing antibodies to HIV and their role in vaccine design","volume":"34","author":"Burton","year":"2016","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0800","doi-asserted-by":"crossref","first-page":"4679","DOI":"10.1111\/febs.13530","article-title":"The HIV glycan shield as a target for broadly neutralizing antibodies","volume":"282","author":"Doores","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0805","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1126\/science.1213256","article-title":"A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield","volume":"334","author":"Pejchal","year":"2011","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0810","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1038\/nature10373","article-title":"Broad neutralization coverage of HIV by multiple highly potent antibodies","volume":"477","author":"Walker","year":"2011","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0815","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1097\/COH.0000000000000153","article-title":"HIV broadly neutralizing antibody targets","volume":"10","author":"Wibmer","year":"2015","journal-title":"Curr. Opin. HIV AIDS"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0820","doi-asserted-by":"crossref","DOI":"10.1016\/j.immuni.2018.02.013","article-title":"A neutralizing antibody recognizing primarily N-linked glycan targets the silent face of the HIV envelope","volume":"48","author":"Zhou","year":"2018","journal-title":"Immunity"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0825","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.str.2018.10.007","article-title":"Structural survey of broadly neutralizing antibodies targeting the HIV-1 Env trimer delineates epitope categories and characteristics of recognition","volume":"27","author":"Chuang","year":"2019","journal-title":"Structure."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0830","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a030262","article-title":"What are the most powerful immunogen design vaccine strategies? Reverse vaccinology 2.0 shows great promise","volume":"9","author":"Burton","year":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0835","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.immuni.2018.04.029","article-title":"HIV-1 vaccines based on antibody identification, B cell ontogeny, and epitope structure","volume":"48","author":"Kwong","year":"2018","journal-title":"Immunity."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0840","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/imr.12481","article-title":"Native-like Env trimers as a platform for HIV-1 vaccine design","volume":"275","author":"Sanders","year":"2017","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0845","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2019.04.016","article-title":"Protein and glycan mimicry in HIV vaccine design","author":"Seabright","year":"2019","journal-title":"J. Mol. Biol."},{"issue":"Suppl. 3","key":"10.1016\/j.bbagen.2019.05.012_bb0850","doi-asserted-by":"crossref","first-page":"C8","DOI":"10.1016\/j.vaccine.2008.04.011","article-title":"Vaccination and antigenic drift in influenza","volume":"26","author":"Boni","year":"2008","journal-title":"Vaccine."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0855","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1093\/molbev\/msr044","article-title":"The genomic rate of molecular adaptation of the human Influenza A virus","volume":"28","author":"Bhatt","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0860","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.1016\/j.jmb.2017.06.015","article-title":"A perspective on the structural and functional constraints for immune evasion: insights from influenza virus","volume":"429","author":"Wu","year":"2017","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0865","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1073\/pnas.81.6.1779","article-title":"A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody","volume":"81","author":"Skehel","year":"1984","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0870","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.virol.2008.03.036","article-title":"Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin","volume":"376","author":"Igarashi","year":"2008","journal-title":"Virology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0875","article-title":"Glycosylation site alteration in the evolution of influenza A (H1N1) viruses","volume":"6","author":"Sun","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2019.05.012_bb0880","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000058","article-title":"Changing selective pressure during antigenic changes in human influenza H3","volume":"4","author":"Blackburne","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0885","doi-asserted-by":"crossref","first-page":"RRN1001","DOI":"10.1371\/currents.RRN1001","article-title":"Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin","volume":"1","author":"Cherry","year":"2009","journal-title":"PLoS Curr."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0890","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.3390\/v6031294","article-title":"Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection","volume":"6","author":"Tate","year":"2014","journal-title":"Viruses."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0895","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001211","article-title":"Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain","volume":"6","author":"Das","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0900","doi-asserted-by":"crossref","first-page":"187ra70","DOI":"10.1126\/scitranslmed.3005996","article-title":"Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses","volume":"5","author":"Medina","year":"2013","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0905","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.3201\/eid2410.171063","article-title":"Molecular evolution, diversity, and adaptation of Influenza A(H7N9) viruses in China","volume":"24","author":"Lu","year":"2018","journal-title":"Emerg. Infect. Dis."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0910","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-06228-8","article-title":"A naturally protective epitope of limited variability as an influenza vaccine target","volume":"9","author":"Thompson","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0915","doi-asserted-by":"crossref","first-page":"E1417","DOI":"10.1073\/pnas.1108754108","article-title":"Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy","volume":"108","author":"Das","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0920","article-title":"Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costs","volume":"14","author":"Kosik","year":"2018","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0925","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1002\/pmic.201100474","article-title":"Comparative characterization of the glycosylation profiles of an influenza hemagglutinin produced in plant and insect hosts","volume":"12","author":"Zhang","year":"2012","journal-title":"Proteomics."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0930","doi-asserted-by":"crossref","first-page":"4027","DOI":"10.1074\/jbc.272.7.4027","article-title":"The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study","volume":"272","author":"Mir-Shekari","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0935","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2018.12.028","article-title":"Unexpected receptor functional mimicry elucidates activation of coronavirus fusion","volume":"176","author":"Walls","year":"2019","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0940","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1126\/science.1234150","article-title":"Rational HIV immunogen design to target specific germline B cell receptors","volume":"340","author":"Jardine","year":"2013","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0945","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3000799","article-title":"Cross-neutralization of 1918 and 2009 Influenza viruses: role of glycans in viral evolution and vaccine design","volume":"2","author":"Wei","year":"2010","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0950","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1126\/science.1186430","article-title":"Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus","volume":"328","author":"Xu","year":"2010","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0955","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02002-17","article-title":"Importance of neutralizing monoclonal antibodies targeting multiple antigenic sites on MERS-CoV Spike to avoid neutralization escape","volume":"92","author":"Wang","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0960","article-title":"Evaluation of candidate vaccine approaches for MERS-CoV","volume":"6","author":"Wang","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0965","doi-asserted-by":"crossref","first-page":"E7348","DOI":"10.1073\/pnas.1707304114","article-title":"Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen","volume":"114","author":"Pallesen","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0970","doi-asserted-by":"crossref","first-page":"14560","DOI":"10.1073\/pnas.0404758101","article-title":"Strategies and mechanisms for host and pathogen survival in acute and persistent viral infections","volume":"101","author":"Hilleman","year":"2004","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0975","doi-asserted-by":"crossref","first-page":"13473","DOI":"10.1038\/ncomms13473","article-title":"Introduction of neutralizing immunogenicity index to the rational design of MERS coronavirus subunit vaccines","volume":"7","author":"Du","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0980","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1007\/s00705-015-2418-y","article-title":"Past, present, and future of arenavirus taxonomy","volume":"160","author":"Radoshitzky","year":"2015","journal-title":"Arch. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0985","doi-asserted-by":"crossref","first-page":"13070","DOI":"10.1128\/JVI.02298-13","article-title":"Crystal structure of Venezuelan Hemorrhagic Fever Virus fusion glycoprotein reveals a class 1 postfusion architecture with extensive glycosylation","volume":"87","author":"Parsy","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0990","doi-asserted-by":"crossref","first-page":"7031","DOI":"10.1073\/pnas.1702127114","article-title":"Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization","volume":"114","author":"Zeltina","year":"2017","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb0995","doi-asserted-by":"crossref","first-page":"8259","DOI":"10.1128\/JVI.00761-09","article-title":"Unusual molecular architecture of the Machupo virus attachment glycoprotein","volume":"83","author":"Bowden","year":"2009","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1000","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00574-17","article-title":"Mutational analysis of Lassa virus glycoprotein highlights regions required for \u03b1-dystroglycan utilization","author":"Acciani","year":"2017","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1005","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005418","article-title":"Acidic pH-induced conformations and LAMP1 binding of the Lassa virus glycoprotein spike","volume":"12","author":"Li","year":"2016","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1010","doi-asserted-by":"crossref","first-page":"621","DOI":"10.2217\/fvl.09.56","article-title":"Ebolavirus glycoprotein structure and mechanism of entry","volume":"4","author":"Lee","year":"2009","journal-title":"Futur. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1015","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1089\/vim.2014.0068","article-title":"The multiple roles of sGP in Ebola pathogenesis","volume":"28","author":"de La Vega","year":"2015","journal-title":"Viral Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1020","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001098","article-title":"Steric shielding of surface epitopes and impaired immune recognition induced by the Ebola virus glycoprotein","volume":"6","author":"Francica","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1025","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nsmb.1435","article-title":"Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2","volume":"15","author":"Bowden","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1030","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/nature17200","article-title":"Pre-fusion structure of a human coronavirus spike protein","volume":"531","author":"Kirchdoerfer","year":"2016","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1035","doi-asserted-by":"crossref","first-page":"4878","DOI":"10.1128\/JVI.80.10.4878-4889.2006","article-title":"N-Glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry","volume":"80","author":"Aguilar","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1040","doi-asserted-by":"crossref","first-page":"11991","DOI":"10.1128\/JVI.01304-12","article-title":"N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralization","volume":"86","author":"Biering","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1045","doi-asserted-by":"crossref","first-page":"11504","DOI":"10.1128\/JVI.01893-13","article-title":"Role of DC-SIGN in Lassa virus entry into human dendritic cells","volume":"87","author":"Goncalves","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1050","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1084\/jem.20021840","article-title":"DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells","volume":"197","author":"Tassaneetrithep","year":"2003","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1055","first-page":"31","article-title":"DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission","volume":"276","author":"Geijtenbeek","year":"2003","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1060","doi-asserted-by":"crossref","first-page":"11992","DOI":"10.1128\/JVI.01094-08","article-title":"Utilization of DC-SIGN for entry of feline coronaviruses into host cells","volume":"82","author":"Regan","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1065","doi-asserted-by":"crossref","first-page":"12090","DOI":"10.1128\/JVI.78.21.12090-12095.2004","article-title":"DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of Severe Acute Respiratory Syndrome Coronavirus","volume":"78","author":"Marzi","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1070","doi-asserted-by":"crossref","first-page":"12022","DOI":"10.1128\/JVI.77.22.12022-12032.2003","article-title":"DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses","volume":"77","author":"Klimstra","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1075","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.chom.2011.06.007","article-title":"DC-SIGN as a receptor for phleboviruses","volume":"10","author":"Lozach","year":"2011","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1080","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/nsmb784","article-title":"Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR","volume":"11","author":"Guo","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1085","doi-asserted-by":"crossref","first-page":"2163","DOI":"10.1126\/science.1066371","article-title":"Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR","volume":"294","author":"Feinberg","year":"2001","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1090","doi-asserted-by":"crossref","first-page":"2990","DOI":"10.1128\/JVI.01705-10","article-title":"N-Linked glycosylation facilitates sialic acid-independent attachment and entry of Influenza A viruses into cells expressing DC-SIGN or L-SIGN","volume":"85","author":"Londrigan","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1095","doi-asserted-by":"crossref","first-page":"14067","DOI":"10.1073\/pnas.0405695101","article-title":"L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus","volume":"101","author":"Cormier","year":"2004","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1100","doi-asserted-by":"crossref","first-page":"15748","DOI":"10.1073\/pnas.0403812101","article-title":"CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus","volume":"101","author":"Jeffers","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1105","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1111\/1574-6976.12052","article-title":"Bitter-sweet symphony: glycan\u2013lectin interactions in virus biology","volume":"38","author":"Van Breedam","year":"2014","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1110","doi-asserted-by":"crossref","first-page":"10244","DOI":"10.1128\/JVI.01662-14","article-title":"Uukuniemi Phlebovirus assembly and secretion leave a functional imprint on the virion glycome","volume":"88","author":"Crispin","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1115","doi-asserted-by":"crossref","first-page":"4384","DOI":"10.1128\/JVI.02628-12","article-title":"Severe fever with thrombocytopenia virus glycoproteins are targeted by neutralizing antibodies and can use DC-SIGN as a receptor for pH-dependent entry into human and animal cell lines","volume":"87","author":"Hofmann","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1120","doi-asserted-by":"crossref","first-page":"149","DOI":"10.3390\/v8050149","article-title":"N-Glycans on the Rift Valley Fever Virus envelope glycoproteins Gn and Gc redundantly support viral infection via DC-SIGN","volume":"8","author":"Phoenix","year":"2016","journal-title":"Viruses."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1125","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.chom.2011.06.007","article-title":"DC-SIGN as a receptor for phleboviruses","volume":"10","author":"Lozach","year":"2011","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1130","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1038\/s41467-017-02789-2","article-title":"Shielding and activation of a viral membrane fusion protein","volume":"9","author":"Halldorsson","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1135","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1111\/tra.12393","article-title":"Differential use of the C-type lectins L-SIGN and DC-SIGN for Phlebovirus endocytosis","volume":"17","author":"L\u00e9ger","year":"2016","journal-title":"Traffic."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1140","doi-asserted-by":"crossref","first-page":"7154","DOI":"10.1073\/pnas.1603827113","article-title":"Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion","volume":"113","author":"Halldorsson","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1145","doi-asserted-by":"crossref","first-page":"e17","DOI":"10.1371\/journal.ppat.0040017","article-title":"The mannose receptor mediates Dengue virus infection of macrophages","volume":"4","author":"Miller","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1150","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.cell.2005.11.042","article-title":"Cryo-EM reconstruction of Dengue virus in complex with the carbohydrate recognition domain of DC-SIGN","volume":"124","author":"Pokidysheva","year":"2006","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1155","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1038\/sj.embor.embor866","article-title":"Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses","volume":"4","author":"Navarro-Sanchez","year":"2003","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1160","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nature02165","article-title":"Structure of the dengue virus envelope protein after membrane fusion","volume":"427","author":"Modis","year":"2004","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1165","doi-asserted-by":"crossref","first-page":"23698","DOI":"10.1074\/jbc.M504337200","article-title":"Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals","volume":"280","author":"Lozach","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1170","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1016\/j.cell.2010.07.038","article-title":"A C-Type lectin collaborates with a CD45 phosphatase homolog to facilitate West Nile virus infection of mosquitoes","volume":"142","author":"Cheng","year":"2010","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1175","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003931","article-title":"Transmission-blocking antibodies against mosquito C-type lectins for Dengue prevention","volume":"10","author":"Liu","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1180","doi-asserted-by":"crossref","first-page":"2861","DOI":"10.4049\/jimmunol.172.5.2861","article-title":"Lassa virus infection of human dendritic cells and macrophages is productive but fails to activate cells","volume":"172","author":"Baize","year":"2004","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1185","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/S0092-8674(00)80694-7","article-title":"DC-SIGN, a dendritic cell\u2013specific HIV-1-binding protein that enhances trans-infection of T cells","volume":"100","author":"Geijtenbeek","year":"2000","journal-title":"Cell."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1190","doi-asserted-by":"crossref","first-page":"5642","DOI":"10.1128\/JVI.78.11.5642-5650.2004","article-title":"pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN","volume":"78","author":"Yang","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1195","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.4049\/jimmunol.168.5.2118","article-title":"The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells","volume":"168","author":"Engering","year":"2002","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1200","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/nm1541","article-title":"Langerin is a natural barrier to HIV-1 transmission by Langerhans cells","volume":"13","author":"de Witte","year":"2007","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1205","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1016\/j.celrep.2017.12.085","article-title":"Mannose receptor 1 restricts HIV particle release from infected macrophages","volume":"22","author":"Sukegawa","year":"2018","journal-title":"Cell Rep."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1210","doi-asserted-by":"crossref","first-page":"E7890","DOI":"10.1073\/pnas.1611213113","article-title":"Substrate recognition and catalysis by GH47 \u03b1-mannosidases involved in Asn-linked glycan maturation in the mammalian secretory pathway","volume":"113","author":"Xiang","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1215","doi-asserted-by":"crossref","first-page":"16088","DOI":"10.1074\/jbc.M200493200","article-title":"Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition","volume":"277","author":"Ng","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1220","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1016\/j.str.2015.07.020","article-title":"Model building and refinement of a natively glycosylated HIV-1 Env protein by high-resolution cryoelectron microscopy","volume":"23","author":"Lee","year":"2015","journal-title":"Structure."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1225","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1126\/science.1083182","article-title":"Antibody domain exchange is an immunological solution to carbohydrate cluster recognition","volume":"300","author":"Calarese","year":"2003","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1230","doi-asserted-by":"crossref","first-page":"10177","DOI":"10.1128\/JVI.01229-14","article-title":"Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy","volume":"88","author":"Murin","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1235","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1038\/333426a0","article-title":"Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid","volume":"333","author":"Weis","year":"1988","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1240","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/289366a0","article-title":"Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 \u00c5 resolution","volume":"289","author":"Wilson","year":"1981","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1245","doi-asserted-by":"crossref","first-page":"4118","DOI":"10.1128\/JVI.03476-12","article-title":"Structural analysis of the evolutionary origins of influenza virus hemagglutinin and other viral lectins","volume":"87","author":"Chen","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1250","first-page":"35","article-title":"Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity","volume":"40","author":"Baum","year":"1990","journal-title":"Acta Histochem. Suppl."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1255","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1146\/annurev.biochem.69.1.531","article-title":"Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin","volume":"69","author":"Skehel","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1260","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1038\/nature05264","article-title":"Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors","volume":"444","author":"Yamada","year":"2006","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1265","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.coviro.2012.03.003","article-title":"The role of receptor binding specificity in interspecies transmission of influenza viruses","volume":"2","author":"Imai","year":"2012","journal-title":"Curr. Opin. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1270","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.tim.2008.01.008","article-title":"Evolving complexities of influenza virus and its receptors","volume":"16","author":"Nicholls","year":"2008","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1275","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1007\/s10719-006-5435-y","article-title":"Role of sialic acids in rotavirus infection","volume":"23","author":"Isa","year":"2006","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1280","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.sbi.2017.04.001","article-title":"Histo-blood group antigens as mediators of infections","volume":"44","author":"Heggelund","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1285","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1007\/s10719-006-5434-z","article-title":"The role of sialic acid in human polyomavirus infections","volume":"23","author":"Gee","year":"2006","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1290","doi-asserted-by":"crossref","first-page":"E8508","DOI":"10.1073\/pnas.1712592114","article-title":"Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein","volume":"114","author":"Li","year":"2017","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1295","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s10719-006-5438-8","article-title":"Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses","volume":"23","author":"de Groot","year":"2006","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1300","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1080\/07853890510007340","article-title":"Glycoconjugate glycans as viral receptors","volume":"37","author":"Olofsson","year":"2005","journal-title":"Ann. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1305","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004146","article-title":"HIV-1 capture and transmission by dendritic cells: The role of viral glycolipids and the cellular receptor siglec-1","volume":"10","author":"Izquierdo-Useros","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1310","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1093\/glycob\/cwv021","article-title":"Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane","volume":"25","author":"Yoshida-Moriguchi","year":"2015","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1315","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1126\/science.1239951","article-title":"SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function","volume":"341","author":"Yoshida-Moriguchi","year":"2013","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1320","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1126\/science.1252480","article-title":"Lassa virus entry requires a trigger-induced receptor switch","volume":"344","author":"Jae","year":"2014","journal-title":"Science (80-.)"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1325","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1126\/science.282.5396.2079","article-title":"Identification of \u03b1-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus","volume":"282","author":"Cao","year":"1998","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1330","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/952387a7-96a0-44f6-98a6-2d7c7b472b0a","article-title":"Old World arenaviruses enter the host cell via the multivesicular body and depend on the endosomal sorting complex required for transport","volume":"7","author":"Pasqual","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1335","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1089\/aid.1993.9.167","article-title":"Cell-surface heparan sulfate proteoglycan mediates HIV-1 infection of T-cell lines","volume":"9","author":"Patel","year":"1993","journal-title":"AIDS Res. Hum. Retrovir."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1340","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1007\/s12250-008-2992-1","article-title":"The importance of heparan sulfate in herpesvirus infection","volume":"23","author":"O'Donnell","year":"2008","journal-title":"Virol. Sin."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1345","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1053\/jhep.2000.18713","article-title":"Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes","volume":"32","author":"Hilgard","year":"2000","journal-title":"Hepatology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1350","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1172\/JCI200113799","article-title":"Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry","volume":"108","author":"Shukla","year":"2001","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1355","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/j.bpj.2017.06.028","article-title":"Binding kinetics and lateral mobility of HSV-1 on end-grafted sulfated glycosaminoglycans","volume":"113","author":"Peerboom","year":"2017","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1360","doi-asserted-by":"crossref","first-page":"21473","DOI":"10.1074\/jbc.M115.637363","article-title":"Mucin-like region of Herpes Simplex Virus type 1 attachment protein glycoprotein C (gC) modulates the virus-glycosaminoglycan interaction","volume":"290","author":"Altg\u00e4rde","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1365","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.immuni.2007.06.008","article-title":"Mammalian N-glycan branching protects against innate immune self-recognition and inflammation in autoimmune disease pathogenesis","volume":"27","author":"Green","year":"2007","journal-title":"Immunity."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1370","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/7045630","article-title":"Mannose-binding lectin: biologic characteristics and role in the susceptibility to infections and ischemia-reperfusion related injury in critically ill neonates","volume":"2017","author":"Auriti","year":"2017","journal-title":"J Immunol Res"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1375","doi-asserted-by":"crossref","first-page":"1733","DOI":"10.1084\/jem.169.5.1733","article-title":"The human mannose-binding protein functions as an opsonin","volume":"169","author":"Kuhlman","year":"1989","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1380","doi-asserted-by":"crossref","first-page":"3930","DOI":"10.1074\/jbc.M111.320341","article-title":"Near-planar solution structures of mannose-binding lectin oligomers provide insight on activation of lectin pathway of complement","volume":"287","author":"Miller","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1385","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1111\/j.1348-0421.1996.tb01156.x","article-title":"The lectin pathway of the complement system","volume":"40","author":"Matsushita","year":"1996","journal-title":"Microbiol. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1390","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.imbio.2006.11.004","article-title":"Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway","volume":"212","author":"Wallis","year":"2007","journal-title":"Immunobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1395","doi-asserted-by":"crossref","first-page":"26058","DOI":"10.1074\/jbc.M401318200","article-title":"Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases","volume":"279","author":"Chen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1400","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1034\/j.1600-065X.2001.1800107.x","article-title":"Ficolins and the lectin complement pathway","volume":"180","author":"Matsushita","year":"2001","journal-title":"Immunol. Rev."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1405","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.chom.2010.07.007","article-title":"Direct complement restriction of Flavivirus infection requires glycan recognition by mannose-binding lectin","volume":"8","author":"Fuchs","year":"2010","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1410","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1046\/j.1365-2567.2003.01707.x","article-title":"Inhibition of DC-SIGN-mediated trans infection of T cells by mannose-binding lectin","volume":"110","author":"Spear","year":"2003","journal-title":"Immunology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1415","doi-asserted-by":"crossref","first-page":"2535","DOI":"10.1099\/vir.0.81199-0","article-title":"Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization","volume":"86","author":"Ji","year":"2005","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1420","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1099\/0022-1317-75-3-615","article-title":"Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin","volume":"75","author":"Anders","year":"1994","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1425","doi-asserted-by":"crossref","first-page":"8753","DOI":"10.1128\/JVI.00554-10","article-title":"A single asparagine-linked glycosylation site of the severe acute respiratory syndrome Coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms","volume":"84","author":"Zhou","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1430","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1513\/pats.200701-018AW","article-title":"Immunomodulatory roles of surfactant proteins A and D: implications in lung disease","volume":"4","author":"Pastva","year":"2007","journal-title":"Proc. Am. Thorac. Soc."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1435","first-page":"L1156","article-title":"Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins","volume":"273","author":"Hartshorn","year":"1997","journal-title":"Am. J. Phys."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1440","doi-asserted-by":"crossref","first-page":"3335","DOI":"10.1021\/bi8022703","article-title":"Recognition of mannosylated ligands and Influenza A virus by human surfactant protein D: contributions of an extended site and residue 343","volume":"48","author":"Crouch","year":"2009","journal-title":"Biochemistry."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1445","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0025005","article-title":"Assessment of the antiviral properties of recombinant porcine SP-D against various Influenza A viruses in vitro","volume":"6","author":"Hillaire","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbagen.2019.05.012_bb1450","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1002\/eji.1830270413","article-title":"Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages","volume":"27","author":"Benne","year":"1997","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1455","doi-asserted-by":"crossref","first-page":"8593","DOI":"10.1128\/JVI.00769-07","article-title":"N-linked glycosylation attenuates H3N2 influenza viruses","volume":"81","author":"Vigerust","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1460","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1099\/vir.0.038414-0","article-title":"Infection of human alveolar macrophages by human coronavirus strain 229E","volume":"93","author":"Funk","year":"2012","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1465","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1165\/rcmb.2003-0107OC","article-title":"Surfactant protein-D enhances phagocytosis and pulmonary clearance of respiratory syncytial virus","volume":"31","author":"LeVine","year":"2004","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1470","doi-asserted-by":"crossref","first-page":"413","DOI":"10.4049\/jimmunol.175.1.413","article-title":"Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines","volume":"175","author":"Levroney","year":"2005","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1475","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000993","article-title":"Endothelial galectin-1 binds to specific glycans on Nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation","volume":"6","author":"Garner","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1480","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1128\/JVI.02435-14","article-title":"Timing of galectin-1 exposure differentially modulates Nipah virus entry and syncytium formation in endothelial cells","volume":"89","author":"Garner","year":"2015","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1485","doi-asserted-by":"crossref","first-page":"10010","DOI":"10.1128\/JVI.00301-11","article-title":"Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis","volume":"85","author":"Yang","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1490","doi-asserted-by":"crossref","first-page":"4120","DOI":"10.4049\/jimmunol.174.7.4120","article-title":"Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells","volume":"174","author":"Ouellet","year":"2005","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1495","doi-asserted-by":"crossref","first-page":"11742","DOI":"10.1128\/JVI.05351-11","article-title":"Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4","volume":"85","author":"St-Pierre","year":"2011","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1500","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.immuni.2014.04.008","article-title":"Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers","volume":"40","author":"Blattner","year":"2014","journal-title":"Immunity."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1505","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1016\/j.immuni.2014.04.009","article-title":"Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers","volume":"40","author":"Falkowska","year":"2014","journal-title":"Immunity."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1510","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1038\/nature13601","article-title":"Broad and potent HIV-1 neutralization by a human antibody that binds the gp41\u2013gp120 interface","volume":"515","author":"Huang","year":"2014","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1515","doi-asserted-by":"crossref","first-page":"7306","DOI":"10.1128\/JVI.76.14.7306-7321.2002","article-title":"The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of \u03b11\u21922 mannose residues on the outer face of gp120","volume":"76","author":"Scanlan","year":"2002","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1520","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1038\/nsmb.2600","article-title":"Structural basis for diverse N-glycan recognition by HIV-1\u2013neutralizing V1\u2013V2\u2013directed antibody PG16","volume":"20","author":"Pancera","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1525","doi-asserted-by":"crossref","first-page":"7325","DOI":"10.1021\/acs.analchem.8b00573","article-title":"Signature of antibody domain exchange by native mass spectrometry and collision-induced unfolding","volume":"90","author":"Watanabe","year":"2018","journal-title":"Anal. Chem."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1530","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/nature14130","article-title":"Recognition determinants of broadly neutralizing human antibodies against dengue viruses","volume":"520","author":"Rouvinski","year":"2015","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1535","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/ni.3058","article-title":"A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus","volume":"16","author":"Dejnirattisai","year":"2015","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1540","doi-asserted-by":"crossref","first-page":"15411","DOI":"10.1038\/ncomms15411","article-title":"Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope","volume":"8","author":"Rouvinski","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1545","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1038\/ni.3515","article-title":"Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with zika virus","volume":"17","author":"Dejnirattisai","year":"2016","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1550","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1126\/science.aat9120","article-title":"Innate immune recognition of glycans targets HIV nanoparticle immunogens to germinal centers","volume":"363","author":"Tokatlian","year":"2019","journal-title":"Science."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1555","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.chembiol.2013.09.010","article-title":"Glycotherapy: new advances inspire a reemergence of glycans in medicine","volume":"21","author":"Hudak","year":"2014","journal-title":"Chem. Biol."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1560","doi-asserted-by":"crossref","first-page":"7490","DOI":"10.1002\/chem.200800700","article-title":"Glycomimetics and glycodendrimers as high affinity microbial anti-adhesins","volume":"14","author":"Imberty","year":"2008","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1565","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1038\/363418a0","article-title":"Rational design of potent sialidase-based inhibitors of influenza virus replication","volume":"363","author":"von Itzstein","year":"1993","journal-title":"Nature."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1570","doi-asserted-by":"crossref","first-page":"93R","DOI":"10.1093\/glycob\/cwg090","article-title":"Glycosidase inhibitors: update and perspectives on practical use","volume":"13","author":"Asano","year":"2003","journal-title":"Glycobiology."},{"key":"10.1016\/j.bbagen.2019.05.012_bb1575","doi-asserted-by":"crossref","first-page":"5774","DOI":"10.1021\/bi800205t","article-title":"Using a 3-O-sulfated heparin octasaccharide to inhibit the entry of herpes simplex virus type 1","volume":"47","author":"Copeland","year":"2008","journal-title":"Biochemistry."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416519301333?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416519301333?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,5]],"date-time":"2025-10-05T03:57:06Z","timestamp":1759636626000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416519301333"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,10]]},"references-count":315,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2019,10]]}},"alternative-id":["S0304416519301333"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2019.05.012","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2019,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Exploitation of glycosylation in enveloped virus pathobiology","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2019.05.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 The Author(s). Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}