{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T16:44:39Z","timestamp":1786985079289,"version":"build-2736575974"},"reference-count":161,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100009526","name":"Amrita Vishwa Vidyapeetham University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009526","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical Pharmacology"],"published-print":{"date-parts":[[2022,12]]},"DOI":"10.1016\/j.bcp.2022.115335","type":"journal-article","created":{"date-parts":[[2022,10,31]],"date-time":"2022-10-31T18:30:00Z","timestamp":1667241000000},"page":"115335","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":37,"special_numbering":"C","title":["Glycosylation in SARS-CoV-2 variants: A path to infection and recovery"],"prefix":"10.1016","volume":"206","author":[{"given":"Arya","family":"Aloor","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajaguru","family":"Aradhya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Parvathy","family":"Venugopal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bipin","family":"Gopalakrishnan Nair","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renuka","family":"Suravajhala","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bcp.2022.115335_b0005","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1128\/MMBR.69.4.635-664.2005","article-title":"Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus","volume":"69","author":"Weiss","year":"2005","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.bcp.2022.115335_b0010","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1002\/jmv.25681","article-title":"Emerging coronaviruses: Genome structure, replication, and pathogenesis","volume":"92","author":"Chen","year":"2020","journal-title":"J. Med. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0015","first-page":"1","article-title":"Sars-cov-2 evolutionary adaptation toward host entry and recognition of receptor o-acetyl sialylation in virus\u2013host interaction","volume":"21","author":"Kim","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0020","doi-asserted-by":"crossref","first-page":"5288","DOI":"10.1128\/JVI.79.9.5288-5295.2005","article-title":"Identification of novel subgenomic RNAs and noncanonical transcription initiation signals of severe acute respiratory syndrome coronavirus","volume":"79","author":"Hussain","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0025","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1016\/j.tim.2015.07.003","article-title":"Sweet talk: protein glycosylation in bacterial interaction with the host","volume":"23","author":"Lu","year":"2015","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.bcp.2022.115335_b0030","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.semcdb.2014.11.005","article-title":"Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum","volume":"41","author":"Shrimal","year":"2015","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0035","first-page":"129","article-title":"Targeting glycans on human pathogens for vaccine design","volume":"428","author":"Krumm","year":"2020","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0040","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1021\/cb9002514","article-title":"Regulation of intracellular signaling by extracellular glycan remodeling","volume":"5","author":"Parker","year":"2010","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0045","doi-asserted-by":"crossref","DOI":"10.3390\/ijms221910577","article-title":"Glycan\u2013lectin interactions in cancer and viral infections and how to disrupt them","volume":"22","author":"Kremsreiter","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0050","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1007\/s12038-010-0073-8","article-title":"Glycan changes: Cancer metastasis and anti-cancer vaccines","volume":"35","author":"Li","year":"2010","journal-title":"J. Biosci."},{"key":"10.1016\/j.bcp.2022.115335_b0055","doi-asserted-by":"crossref","first-page":"3109","DOI":"10.1016\/j.cell.2021.04.023","article-title":"Small RNAs are modified with N-glycans and displayed on the surface of living cells","volume":"184","author":"Flynn","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0060","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.sbi.2019.11.004","article-title":"Glycan structures and their interactions with proteins. A NMR view","volume":"62","author":"Gimeno","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0065","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2018.02754","article-title":"Glycans as key checkpoints of T cell activity and function","volume":"9","author":"Pereira","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0070","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1016\/j.cell.2018.02.054","article-title":"Common features of enveloped viruses and implications for immunogen design for next-generation vaccines","volume":"172","author":"Rey","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0075","doi-asserted-by":"crossref","DOI":"10.1016\/j.scib.2021.01.010","article-title":"Binding of the SARS-CoV-2 spike protein to glycans","author":"Hao","year":"2021","journal-title":"Sci. Bull."},{"key":"10.1016\/j.bcp.2022.115335_b0080","doi-asserted-by":"crossref","first-page":"12910","DOI":"10.1074\/jbc.REV120.013930","article-title":"The molecular virology of coronaviruses","volume":"295","author":"Hartenian","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0085","doi-asserted-by":"crossref","unstructured":"Mehdipour, A. R. & Hummer, G. Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike. bioRxiv (2020), doi: 10.1101\/2020.07.09.193680.","DOI":"10.1101\/2020.07.09.193680"},{"key":"10.1016\/j.bcp.2022.115335_b0090","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmb.2020.166762","article-title":"Subtle influence of ACE2 glycan processing on SARS-CoV-2 recognition","volume":"433","author":"Allen","year":"2021","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0095","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1021\/acscentsci.0c01056","article-title":"Beyond shielding: the roles of glycans in the SARS-CoV-2 spike protein","volume":"6","author":"Casalino","year":"2020","journal-title":"ACS Cent. Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0100","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mBio.00584-16","article-title":"Lectin-glycan interaction network-based identification of host receptors of microbial pathogenic adhesins","volume":"7","author":"Ielasi","year":"2016","journal-title":"MBio"},{"key":"10.1016\/j.bcp.2022.115335_b0105","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1016\/j.jmb.2019.04.016","article-title":"Protein and glycan mimicry in HIV vaccine design","volume":"431","author":"Seabright","year":"2019","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0110","doi-asserted-by":"crossref","DOI":"10.3390\/md17080440","article-title":"Mannose-specific lectins from marine algae: diverse structural scaffolds associated to common virucidal and anti-cancer properties","volume":"17","author":"Barre","year":"2019","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.bcp.2022.115335_b0115","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1371\/journal.ppat.1004401","article-title":"A sialic acid binding site in a human picornavirus","volume":"10","author":"Zocher","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bcp.2022.115335_b0120","doi-asserted-by":"crossref","first-page":"10408","DOI":"10.1128\/JVI.01155-12","article-title":"Glycan binding avidity determines the systemic fate of adeno-associated virus type 9","volume":"86","author":"Shen","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0125","unstructured":"J. Ahn, Y.Q. Yu, M. Gilar, Corporation, W. UPLC-FLR Method Development of 2-AB Labeled Glycan Separation in Hydrophilic Interaction Chromatography (HILIC), 6\u20139."},{"key":"10.1016\/j.bcp.2022.115335_b0130","doi-asserted-by":"crossref","unstructured":"N.R. Council, Transforming Glycoscience. Transforming Glycoscience: A Roadmap for the Future, National Academies Press, 2012, doi: 10.17226\/13446.","DOI":"10.17226\/13446"},{"key":"10.1016\/j.bcp.2022.115335_b0135","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s13337-015-0293-5","article-title":"Viral glycoproteins: biological role and application in diagnosis","volume":"27","author":"Banerjee","year":"2016","journal-title":"VirusDisease"},{"key":"10.1016\/j.bcp.2022.115335_b0140","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.cell.2020.02.058","article-title":"Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein","volume":"181","author":"Walls","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0145","doi-asserted-by":"crossref","first-page":"2299","DOI":"10.1021\/ac00171a028","article-title":"Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons","volume":"60","author":"Karas","year":"1988","journal-title":"Anal. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0150","doi-asserted-by":"crossref","unstructured":"J.B. Fenn, M. Mann, C.K. Meng, S.F. Wong, C.M. Whitehouse, Electrospray ionization for mass spectrometry of large biomolecules, Science (80-.) 246 (1989) 64\u201371.","DOI":"10.1126\/science.2675315"},{"key":"10.1016\/j.bcp.2022.115335_b0155","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1002\/jssc.200900771","article-title":"Enhanced glyco-profiling by specific glycopeptide enrichment and complementary monolithic nano-LC (ZIC-HILIC\/RP18e)\/ESI-MS analysis","volume":"33","author":"Wohlgemuth","year":"2010","journal-title":"J. Sep. Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0160","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1080\/19420862.2017.1290033","article-title":"Resolving the micro-heterogeneity and structural integrity of monoclonal antibodies by hybrid mass spectrometric approaches","volume":"9","author":"Yang","year":"2017","journal-title":"MAbs"},{"key":"10.1016\/j.bcp.2022.115335_b0165","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1002\/mas.21679","article-title":"Recent advancements in glycoproteomic studies: Glycopeptide enrichment and derivatization, characterization of glycosylation in SARS CoV2, and interacting glycoproteins","volume":"41","author":"Puji\u0107","year":"2022","journal-title":"Mass Spectrom. Rev."},{"key":"10.1016\/j.bcp.2022.115335_b0170","doi-asserted-by":"crossref","unstructured":"Y. Watanabe, J.D. Allen, D. Wrapp, J.S. McLellan, M. Crispin, Site-specific glycan analysis of the SARS-CoV-2 spike, Science (80-.) 369 (2020) 330\u2013333.","DOI":"10.1126\/science.abb9983"},{"key":"10.1016\/j.bcp.2022.115335_b0175","first-page":"1","article-title":"N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry","volume":"11","author":"Wang","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2022.115335_b0180","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jaut.2014.12.002","article-title":"Glycans in the immune system and the altered glycan theory of autoimmunity: a critical review","volume":"48","author":"Maverakis","year":"2015","journal-title":"J. Autoimmun."},{"key":"10.1016\/j.bcp.2022.115335_b0185","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmolb.2021.629873","article-title":"Glycans of SARS-CoV-2 spike protein in virus infection and antibody production","volume":"8","author":"Zhao","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bcp.2022.115335_b0190","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1021\/acsptsci.1c00015","article-title":"Glycosylation of SARS-CoV-2 steers evolutionary outcomes in the postvaccination phase","volume":"4","author":"Fern\u00e1ndez","year":"2021","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0195","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12967-018-1695-0","article-title":"N-glycosylation patterns of plasma proteins and immunoglobulin G in chronic obstructive pulmonary disease","volume":"16","author":"Pavi\u0107","year":"2018","journal-title":"J. Transl. Med."},{"key":"10.1016\/j.bcp.2022.115335_b0200","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0196163","article-title":"Changes in N-glycans of IgG4 and its relationship with the existence of hypocomplementemia and individual organ involvement in patients with IgG4-related disease","volume":"13","author":"Konno","year":"2018","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bcp.2022.115335_b0205","unstructured":"E.I. Patterson, G.L. Hughes, I.C. Almeida, T. Zech, \u00c1. Acosta-serrano, Inhibition of Protein N- Glycosylation Blocks SARS-CoV-2 Infection (2022)."},{"key":"10.1016\/j.bcp.2022.115335_b0210","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.103272","article-title":"The effect of N-glycosylation of SARS-CoV-2 spike protein on the virus interaction with the host cell ACE2 receptor","volume":"24","author":"Huang","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.bcp.2022.115335_b0215","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2003138117","article-title":"Cell entry mechanisms of SARS-CoV-2","volume":"117","author":"Shang","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bcp.2022.115335_b0220","article-title":"The role of cell surface sialic acids for SARS-CoV-2 infection","volume":"2021","author":"Sun","year":"2021","journal-title":"Glycobiology"},{"key":"10.1016\/j.bcp.2022.115335_b0225","doi-asserted-by":"crossref","unstructured":"P. V\u2019kovski, A. Kratzel, S. Steiner, H. Stalder, V. Thiel, Coronavirus biology and replication: implications for SARS-CoV-2, Nat. Rev. Microbiol. 19 (2021) 155\u2013170.","DOI":"10.1038\/s41579-020-00468-6"},{"key":"10.1016\/j.bcp.2022.115335_b0230","doi-asserted-by":"crossref","unstructured":"V. Ruocco, R. Strasser, Transient Expression of Glycosylated SARS-CoV-2 Antigens in Nicotiana benthamiana. (2022).","DOI":"10.3390\/plants11081093"},{"key":"10.1016\/j.bcp.2022.115335_b0235","doi-asserted-by":"crossref","unstructured":"Y. Huang, C. Yang, X.f. Xu, W. Xu, S.w. Liu, Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19, Acta Pharmacol. Sin. 41 (2020) 1141\u20131149.","DOI":"10.1038\/s41401-020-0485-4"},{"key":"10.1016\/j.bcp.2022.115335_b0240","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/s41564-021-00908-w","article-title":"The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets","volume":"6","author":"Peacock","year":"2021","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.bcp.2022.115335_b0245","article-title":"Functional evaluation of proteolytic activation for the SARS-CoV-2 variant B.1.1.7: role of the P681H mutation","volume":"1\u201328","author":"Lubinski","year":"2021","journal-title":"SSRN Electron. J."},{"key":"10.1016\/j.bcp.2022.115335_b0250","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2020.576622","article-title":"The SARS-CoV-2 spike glycoprotein biosynthesis, structure, function, and antigenicity: implications for the design of spike-based vaccine immunogens","volume":"11","author":"Duan","year":"2020","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0255","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.ppat.1009282","article-title":"Multimerization- and glycosylation-dependent receptor binding of SARS-CoV-2 spike proteins","volume":"17","author":"Bouwman","year":"2021","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bcp.2022.115335_b0260","doi-asserted-by":"crossref","first-page":"6078","DOI":"10.1128\/JVI.00074-08","article-title":"Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation","volume":"82","author":"de Haan","year":"2008","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0265","doi-asserted-by":"crossref","unstructured":"D. Wrapp, et al., Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation, Science (80-.) 367 (2020) 1260\u20131263.","DOI":"10.1126\/science.abb2507"},{"key":"10.1016\/j.bcp.2022.115335_b0270","doi-asserted-by":"crossref","first-page":"5913","DOI":"10.1128\/JVI.78.11.5913-5922.2004","article-title":"Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site","volume":"78","author":"Lontok","year":"2004","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0275","first-page":"20","article-title":"Natural flavonoids as potential for anti-SARS-CoV-2","volume":"2","author":"Inhibitors","year":"2020","journal-title":"Mdpi"},{"key":"10.1016\/j.bcp.2022.115335_b0280","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmgm.2020.107716","article-title":"Virtual screening and molecular dynamics study of approved drugs as inhibitors of spike protein S1 domain and ACE2 interaction in SARS-CoV-2","volume":"101","author":"Prajapat","year":"2020","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.bcp.2022.115335_b0285","doi-asserted-by":"crossref","DOI":"10.1016\/j.mehy.2020.109984","article-title":"Aminoglycosides can be a better choice over macrolides in COVID-19 regimen: Plausible mechanism for repurposing strategy","volume":"144","author":"Chalichem","year":"2020","journal-title":"Med. Hypotheses"},{"key":"10.1016\/j.bcp.2022.115335_b0290","article-title":"Transmembrane protease serine 2 proteolytic cleavage of the SARS-CoV-2 spike protein: a mechanistic quantum mechanics\/molecular mechanics study to inspire the design of new drugs to fight the COVID-19 pandemic","volume":"2022","author":"Teixeira","year":"2022","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.bcp.2022.115335_b0295","first-page":"1","article-title":"Ace2: evidence of role as entry receptor for sars-cov-2 and implications in comorbidities","volume":"9","author":"Cuervo","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.bcp.2022.115335_b0300","doi-asserted-by":"crossref","DOI":"10.1038\/s41392-021-00558-8","article-title":"Cathepsin L plays a key role in SARS-CoV-2 infection in humans and humanized mice and is a promising target for new drug development","volume":"6","author":"Zhao","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"10.1016\/j.bcp.2022.115335_b0305","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/s41422-020-0282-0","article-title":"Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro","volume":"30","author":"Wang","year":"2020","journal-title":"Cell Res."},{"key":"10.1016\/j.bcp.2022.115335_b0310","doi-asserted-by":"crossref","unstructured":"Q. Yang, et al., Inhibition of SARS-CoV-2 viral entry in vitro upon blocking N- and O-glycan elaboration, bioRxiv 1\u201319 (2020), doi: 10.1101\/2020.10.15.339838.","DOI":"10.1101\/2020.10.15.339838"},{"key":"10.1016\/j.bcp.2022.115335_b0315","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/s41581-019-0129-4","article-title":"Glycosylation in health and disease","volume":"15","author":"Reily","year":"2019","journal-title":"Nat. Rev. Nephrol."},{"key":"10.1016\/j.bcp.2022.115335_b0320","doi-asserted-by":"crossref","first-page":"2418","DOI":"10.1128\/JVI.02146-06","article-title":"The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein","volume":"81","author":"McBride","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0325","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.R120.002093","article-title":"Meta-heterogeneity: evaluating and describing the diversity in glycosylation between sites on the same glycoprotein","volume":"20","author":"\u010caval","year":"2021","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bcp.2022.115335_b0330","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-021-21983-x","article-title":"A slowly cleaved viral signal peptide acts as a protein-integral immune evasion domain","volume":"12","author":"Seidel","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2022.115335_b0335","doi-asserted-by":"crossref","unstructured":"A.S. Heffron, S.J. Mcilwain, M.F. Amjadi, D.A. Baker, The landscape of antibody binding in SARS-CoV-2 infection, SARS-CoV-2 antibody binding landscape. (2021).","DOI":"10.1101\/2020.10.10.334292"},{"key":"10.1016\/j.bcp.2022.115335_b0340","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/s41586-020-2180-5","article-title":"Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor","volume":"581","author":"Lan","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2022.115335_b0345","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1093\/glycob\/cwaa042","article-title":"Deducing the N- And O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2","volume":"30","author":"Shajahan","year":"2020","journal-title":"Glycobiology"},{"key":"10.1016\/j.bcp.2022.115335_b0350","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/s41586-020-2286-9","article-title":"A SARS-CoV-2 protein interaction map reveals targets for drug repurposing","volume":"583","author":"Gordon","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2022.115335_b0355","doi-asserted-by":"crossref","first-page":"41931","DOI":"10.1074\/jbc.M112.418210","article-title":"Crystal structure of bovine coronavirus spike protein lectin domain","volume":"287","author":"Peng","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0360","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.1016\/j.bbamcr.2013.04.001","article-title":"N-linked protein glycosylation in the ER","volume":"1833","author":"Aebi","year":"2013","journal-title":"Biochim. Biophys. Acta - Mol. Cell Res."},{"key":"10.1016\/j.bcp.2022.115335_b0365","doi-asserted-by":"crossref","first-page":"23763","DOI":"10.1002\/anie.202011015","article-title":"Structural characterization of N-linked glycans in the receptor binding domain of the SARS-CoV-2 spike protein and their interactions with human lectins","volume":"59","author":"Lenza","year":"2020","journal-title":"Angew. Chemie - Int. Ed."},{"key":"10.1016\/j.bcp.2022.115335_b0370","doi-asserted-by":"crossref","first-page":"4357","DOI":"10.1021\/acs.jproteome.1c00323","article-title":"Direct comparison of N-glycans and their isomers derived from spike glycoprotein 1 of MERS-CoV, SARS-CoV-1, and SARS-CoV-2","volume":"20","author":"Cho","year":"2021","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bcp.2022.115335_b0375","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2021.691715","article-title":"Epitope classification and RBD binding properties of neutralizing antibodies against SARS-CoV-2 variants of concern","volume":"12","author":"Deshpande","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0380","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1021\/acs.analchem.0c03173","article-title":"N-and O-glycosylation of the SARS-CoV-2 spike protein","volume":"93","author":"Sanda","year":"2021","journal-title":"Anal. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0385","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1038\/sj.emboj.7600640","article-title":"Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2","volume":"24","author":"Li","year":"2005","journal-title":"EMBO J."},{"key":"10.1016\/j.bcp.2022.115335_b0390","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.3390\/v4061011","article-title":"Mechanisms of coronavirus cell entry mediated by the viral spike protein","volume":"4","author":"Belouzard","year":"2012","journal-title":"Viruses"},{"key":"10.1016\/j.bcp.2022.115335_b0395","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1038\/s41589-020-0551-8","article-title":"Selective N-glycan editing on living cell surfaces to probe glycoconjugate function","volume":"16","author":"Tang","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0400","article-title":"Analysis of SARS-CoV-2 spike glycosylation reveals shedding of a vaccine candidate","author":"Brun","year":"2020","journal-title":"bioRxiv"},{"key":"10.1016\/j.bcp.2022.115335_b0405","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/v13040551","article-title":"Site-specific o-glycosylation analysis of sars-cov-2 spike protein produced in insect and human cells","volume":"13","author":"Bagdonaite","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.bcp.2022.115335_b0410","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1038\/s41422-021-00545-2","article-title":"O-glycosylation pattern of the SARS-CoV-2 spike protein reveals an \u201cO-Follow-N\u201d rule","volume":"31","author":"Tian","year":"2021","journal-title":"Cell Res."},{"key":"10.1016\/j.bcp.2022.115335_b0415","doi-asserted-by":"crossref","first-page":"342","DOI":"10.20411\/pai.v5i1.377","article-title":"The structure of the membrane protein of sars-cov-2 resembles the sugar transporter semisweet","volume":"5","author":"Thomas","year":"2020","journal-title":"Pathog. Immun."},{"key":"10.1016\/j.bcp.2022.115335_b0420","doi-asserted-by":"crossref","first-page":"2326","DOI":"10.1128\/JVI.80.5.2326-2336.2006","article-title":"Glycosylation of the severe acute respiratory syndrome coronavirus triple-spanning membrane proteins 3a and M","volume":"80","author":"Oostra","year":"2006","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0425","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-021-21953-3","article-title":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA","volume":"12","author":"Cubuk","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2022.115335_b0430","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1002\/pro.4075","article-title":"Characterization of the SARS-CoV-2 E Protein: Sequence, Structure, Viroporin, and Inhibitors","volume":"30","author":"Cao","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.bcp.2022.115335_b0435","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/s41586-020-2179-y","article-title":"Structural basis of receptor recognition by SARS-CoV-2","volume":"581","author":"Shang","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2022.115335_b0440","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-19808-4","article-title":"SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity","volume":"11","author":"Zhang","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2022.115335_b0445","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/s41423-021-00836-z","article-title":"Increased immune escape of the new SARS-CoV-2 variant of concern Omicron","volume":"19","author":"Hu","year":"2022","journal-title":"Cell. Mol. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0450","doi-asserted-by":"crossref","first-page":"1618","DOI":"10.1016\/S0140-6736(22)00327-0","article-title":"Symptom prevalence, duration, and risk of hospital admission in individuals infected with SARS-CoV-2 during periods of omicron and delta variant dominance: a prospective observational study from the ZOE COVID Study","volume":"399","author":"Menni","year":"2022","journal-title":"Lancet"},{"key":"10.1016\/j.bcp.2022.115335_b0455","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1056\/NEJMc2202092","article-title":"Duration of shedding of culturable virus in SARS-CoV-2 omicron (BA.1) infection","volume":"387","author":"Boucau","year":"2022","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bcp.2022.115335_b0460","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2021.830527","article-title":"Omicron: a heavily mutated SARS-CoV-2 variant exhibits stronger binding to ACE2 and potently escapes approved COVID-19 therapeutic antibodies","volume":"12","author":"Shah","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0465","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15252\/msb.20209610","article-title":"The protein expression profile of ACE2 in human tissues","volume":"16","author":"Hikmet","year":"2020","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0470","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1002\/path.1570","article-title":"Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis","volume":"203","author":"Hamming","year":"2004","journal-title":"J. Pathol."},{"key":"10.1016\/j.bcp.2022.115335_b0475","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejim.2021.09.007","article-title":"The pivotal link between ACE2 deficiency and SARS-CoV-2 infection: one year later","author":"Angeli","year":"2021","journal-title":"Eur. J. Intern. Med."},{"key":"10.1016\/j.bcp.2022.115335_b0480","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/307315","article-title":"Angiotensin-converting enzyme 2: the first decade","volume":"2012","author":"Clarke","year":"2012","journal-title":"Int. J. Hypertens."},{"key":"10.1016\/j.bcp.2022.115335_b0485","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13054-020-03120-0","article-title":"Role of angiotensin-converting enzyme 2 (ACE2) in COVID-19","volume":"24","author":"Ni","year":"2020","journal-title":"Crit. Care"},{"key":"10.1016\/j.bcp.2022.115335_b0490","doi-asserted-by":"crossref","first-page":"7336","DOI":"10.1021\/acs.jpcb.0c04511","article-title":"Does SARS-CoV-2 bind to human ACE2 more strongly than does SARS-CoV?","volume":"124","author":"Nguyen","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bcp.2022.115335_b0495","doi-asserted-by":"crossref","first-page":"5949","DOI":"10.1039\/D1CC02305E","article-title":"ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV","volume":"57","author":"Acharya","year":"2021","journal-title":"Chem. Commun."},{"key":"10.1016\/j.bcp.2022.115335_b0500","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2021.683800","article-title":"SARS-CoV-2\/ACE2 interaction suppresses IRAK-M expression and promotes pro-inflammatory cytokine production in macrophages","volume":"12","author":"Pantazi","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0505","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1093\/glycob\/cwaa101","article-title":"Comprehensive characterization of N- and O- glycosylation of SARS-CoV-2 human receptor angiotensin converting enzyme 2","volume":"31","author":"Shajahan","year":"2021","journal-title":"Glycobiology"},{"key":"10.1016\/j.bcp.2022.115335_b0510","unstructured":"Peng Zhao1,#, Jeremy L. Praissman1,#, Oliver C. Grant1,#, Yongfei Cai2, Tianshu Xiao2, Katelyn E. Rosenbalm1, Kazuhiro Aoki1, Benjamin P. Kellman3, Robert Bridger1, Dan H. Barouch4, Melinda 6 A. Brindley5, Nathan E. Lewis3, 6, Michael Tiemeyer1, Bing Chen, and L. 7 W. Virus-receptor interactions of glycosylated SARS-CoV-2 spike and Human ACE2 receptor, Phys. Educ. 23 (2017) 1\u201310."},{"key":"10.1016\/j.bcp.2022.115335_b0515","unstructured":"D. McMaster, M. Veremu, K. Jonas, Co Sc. Int. Soc. Travel Med. (2020) 1\u201356."},{"key":"10.1016\/j.bcp.2022.115335_b0520","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fcimb.2018.00280","article-title":"The sialic acid binding activity of human parainfluenza virus 3 and mumps virus glycoproteins enhances the adherence of group B streptococci to HEp-2 cells","volume":"8","author":"Tong","year":"2018","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.bcp.2022.115335_b0525","doi-asserted-by":"crossref","DOI":"10.3390\/biom11060831","article-title":"Sialic acids as receptors for pathogens","volume":"11","author":"Burzy\u0144ska","year":"2021","journal-title":"Biomolecules"},{"key":"10.1016\/j.bcp.2022.115335_b0530","doi-asserted-by":"crossref","first-page":"3730","DOI":"10.1128\/JVI.02148-09","article-title":"Macrophage receptors for influenza A virus: role of the macrophage galactose-type lectin and mannose receptor in viral entry","volume":"84","author":"Upham","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0535","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/s41589-021-00924-1","article-title":"Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2","volume":"18","author":"Nguyen","year":"2022","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bcp.2022.115335_b0540","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/s10719-021-10021-z","article-title":"SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection","volume":"38","author":"Trbojevi\u0107-Akma\u010di\u0107","year":"2021","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.bcp.2022.115335_b0545","doi-asserted-by":"crossref","first-page":"21","DOI":"10.4081\/hr.2021.8857","article-title":"Heparin-induced thrombocy-topenia and covid-19","volume":"13","author":"Sartori","year":"2021","journal-title":"Hematol. Rep."},{"key":"10.1016\/j.bcp.2022.115335_b0550","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.cell.2020.09.033","article-title":"SARS-CoV-2 infection depends on cellular heparan sulfate and ACE2","volume":"183","author":"Clausen","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0555","doi-asserted-by":"crossref","DOI":"10.1016\/j.antiviral.2020.104873","article-title":"Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions","volume":"181","author":"Kim","year":"2020","journal-title":"Antiviral Res."},{"key":"10.1016\/j.bcp.2022.115335_b0560","doi-asserted-by":"crossref","unstructured":"F. Zhang, Z. Zhang, R.J. Linhardt, Chapter 3 \u2013 Glycosaminoglycans, Handb. Glycomics 59\u201380 (2010), doi: 10.1016\/B978-0-12-373600-0.00003-2. Get rights and content.","DOI":"10.1016\/B978-0-12-373600-0.00003-2"},{"key":"10.1016\/j.bcp.2022.115335_b0565","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01987-20","article-title":"Effective inhibition of SARS-CoV-2 entry by heparin and enoxaparin derivatives","volume":"95","author":"Tandon","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0570","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1002\/rth2.12353","article-title":"Using heparin molecules to manage COVID-2019","volume":"4","author":"Liu","year":"2020","journal-title":"Res. Pract. Thromb. Haemost."},{"key":"10.1016\/j.bcp.2022.115335_b0575","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1038\/s41422-020-00460-y","article-title":"AXL is a candidate receptor for SARS-CoV-2 that promotes infection of pulmonary and bronchial epithelial cells","volume":"31","author":"Wang","year":"2021","journal-title":"Cell Res."},{"key":"10.1016\/j.bcp.2022.115335_b0580","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/j.molcel.2020.04.022","article-title":"A multibasic cleavage site in the spike protein of SARS-CoV-2 is essential for infection of human lung cells","volume":"78","author":"Hoffmann","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0585","doi-asserted-by":"crossref","DOI":"10.3389\/fgene.2021.667231","article-title":"Transmembrane serine protease 2 polymorphisms and susceptibility to severe acute respiratory syndrome coronavirus type 2 infection: a German case-control study","volume":"12","author":"Sch\u00f6nfelder","year":"2021","journal-title":"Front. Genet."},{"key":"10.1016\/j.bcp.2022.115335_b0590","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1126\/sciimmunol.abc3582","article-title":"TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes","volume":"5","author":"Zang","year":"2020","journal-title":"Sci. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0595","doi-asserted-by":"crossref","unstructured":"S. Ravichandran, et al., Antibody signature induced by SARS-CoV-2 spike protein immunogens in rabbits, 3539 (2020) 1\u20139.","DOI":"10.1101\/2020.05.12.091918"},{"key":"10.1016\/j.bcp.2022.115335_b0600","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/v13010109","article-title":"Domains and functions of spike protein in sars-cov-2 in the context of vaccine design","volume":"13","author":"Xia","year":"2021","journal-title":"Viruses"},{"key":"10.1016\/j.bcp.2022.115335_b0605","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/vaccines9010039","article-title":"A covid-19 vaccine: big strides come with big challenges","volume":"9","author":"Mellet","year":"2021","journal-title":"Vaccines"},{"key":"10.1016\/j.bcp.2022.115335_b0610","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.bcp.2022.115335_b0615","doi-asserted-by":"crossref","DOI":"10.1084\/jem.20211003","article-title":"Glycan engineering of the sars-cov-2 receptor-binding domain elicits cross-neutralizing antibodies for sars-related viruses","volume":"218","author":"Shinnakasu","year":"2021","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bcp.2022.115335_b0620","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.immuni.2018.04.029","article-title":"Review HIV-1 vaccines based on antibody identification","volume":"48","author":"Ontogeny","year":"2018","journal-title":"Immunity"},{"key":"10.1016\/j.bcp.2022.115335_b0625","first-page":"19","article-title":"Application note glycosylation of the receptor binding domain of covid-19 virus spike","volume":"2020","author":"Note","year":"2019","journal-title":"Protein"},{"key":"10.1016\/j.bcp.2022.115335_b0630","doi-asserted-by":"crossref","unstructured":"F. Chiodo, et al., Novel ACE2-independent carbohydrate-binding of SARS-CoV-2 spike protein to host lectins and lung microbiota, bioRxiv (2020) 2020.05.13.092478.","DOI":"10.1101\/2020.05.13.092478"},{"key":"10.1016\/j.bcp.2022.115335_b0635","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/nrmicro2538","article-title":"Mucin dynamics and enteric pathogens","volume":"9","author":"McGuckin","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.bcp.2022.115335_b0640","doi-asserted-by":"crossref","unstructured":"P. Van den Steen, P.M. Rudd, R.A. Dwek, G. Opdenakker, Mucin glycans attenuate the virulence of Pseudomonas aeruginosa in infection, Crit. Rev. Biochem. Mol. Biol. 33 (1998) 151\u2013208.","DOI":"10.1080\/10409239891204198"},{"key":"10.1016\/j.bcp.2022.115335_b0645","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1146\/annurev.physiol.70.113006.100702","article-title":"Structure and function of the polymeric mucins in airways mucus","volume":"70","author":"Thornton","year":"2008","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.bcp.2022.115335_b0650","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ejpb.2016.01.005","article-title":"N-glycosylation heterogeneity and the influence on structure, function and pharmacokinetics of monoclonal antibodies and Fc fusion proteins","volume":"100","author":"Higel","year":"2016","journal-title":"Eur. J. Pharm. Biopharm."},{"key":"10.1016\/j.bcp.2022.115335_b0655","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1128\/JVI.72.3.2253-2258.1998","article-title":"Enhanced virus clearance by early inducible lymphocytic choriomeningitis virus-neutralizing antibodies in immunoglobulin-transgenic mice","volume":"72","author":"Seiler","year":"1998","journal-title":"J. Virol."},{"key":"10.1016\/j.bcp.2022.115335_b0660","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1128\/CVI.00374-14","article-title":"Influenza virus-specific neutralizing IgM antibodies persist for a lifetime","volume":"21","author":"Skountzou","year":"2014","journal-title":"Clin. Vaccine Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0665","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2021.748566","article-title":"Profile of immunoglobulin G N-glycome in COVID-19 patients: a case-control study","volume":"12","author":"Hou","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0670","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/s41590-020-00828-7","article-title":"Proinflammatory IgG Fc structures in patients with severe COVID-19","volume":"22","author":"Chakraborty","year":"2021","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0675","doi-asserted-by":"crossref","DOI":"10.1182\/blood.2021011871","article-title":"Aberrant glycosylation of anti-SARS-CoV-2 IgG is a pro-thrombotic stimulus for platelets","author":"Bye","year":"2021","journal-title":"Blood"},{"key":"10.1016\/j.bcp.2022.115335_b0680","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1016\/j.cell.2021.03.028","article-title":"N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2","volume":"184","author":"McCallum","year":"2021","journal-title":"Cell"},{"key":"10.1016\/j.bcp.2022.115335_b0685","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-16567-0","article-title":"Vulnerabilities in coronavirus glycan shields despite extensive glycosylation","volume":"11","author":"Watanabe","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2022.115335_b0690","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-12495-0","article-title":"Subclass-specific IgG glycosylation is associated with markers of inflammation and metabolic health","volume":"7","author":"Plomp","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2022.115335_b0695","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1111\/jth.15275","article-title":"Antibody-mediated platelet activation in COVID-19: a coincidence or a new mechanism of the dysregulated coagulation system?","volume":"19","author":"Althaus","year":"2021","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.bcp.2022.115335_b0700","doi-asserted-by":"crossref","first-page":"26733","DOI":"10.1074\/jbc.M202069200","article-title":"Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fc\u03b3RIII and antibody-dependent cellular toxicity","volume":"277","author":"Shields","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0705","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1093\/glycob\/cwn093","article-title":"Inhibition of the interaction between the SARS-CoV Spike protein and its cellular receptor by anti-histo-blood group antibodies","volume":"18","author":"Guillon","year":"2008","journal-title":"Glycobiology"},{"key":"10.1016\/j.bcp.2022.115335_b0710","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1007\/s00277-021-04489-w","article-title":"Association between ABO blood types and coronavirus disease 2019 (COVID-19), genetic associations, and underlying molecular mechanisms: a literature review of 23 studies","volume":"100","author":"Zhang","year":"2021","journal-title":"Ann. Hematol."},{"key":"10.1016\/j.bcp.2022.115335_b0715","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2018.00590","article-title":"C-type lectin receptors in antiviral immunity and viral escape","volume":"9","author":"Bermejo-Jambrina","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0720","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/nri2569","article-title":"Signalling through C-type lectin receptors: shaping immune responses","volume":"9","author":"Geijtenbeek","year":"2009","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0725","doi-asserted-by":"crossref","first-page":"23971","DOI":"10.1002\/ange.202011015","article-title":"Structural characterization of N-linked glycans in the receptor binding domain of the SARS-CoV-2 spike protein and their interactions with human lectins","volume":"132","author":"Lenza","year":"2020","journal-title":"Angew. Chemie"},{"key":"10.1016\/j.bcp.2022.115335_b0730","doi-asserted-by":"crossref","first-page":"28939","DOI":"10.1074\/jbc.M104565200","article-title":"A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR","volume":"276","author":"Mitchell","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2022.115335_b0735","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1093\/intimm\/dxh246","article-title":"Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells","volume":"17","author":"van Vliet","year":"2005","journal-title":"Int. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0740","doi-asserted-by":"crossref","unstructured":"H. Blanchard, P.M. Collins, Galectin-3 inhibitors: a patent review (2008 \u2013 present), (2014) 13543776.","DOI":"10.1517\/13543776.2014.947961"},{"key":"10.1016\/j.bcp.2022.115335_b0745","doi-asserted-by":"crossref","unstructured":"C. Gao, et al., SARS-CoV-2 spike protein interacts with multiple innate immune receptors, bioRxiv Prepr. Serv. Biol. (2020) 227462, doi: 10.1101\/2020.07.29.227462.","DOI":"10.1101\/2020.07.29.227462"},{"key":"10.1016\/j.bcp.2022.115335_b0750","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev-immunol-102419-035900","article-title":"Siglecs as immune cell checkpoints in disease","volume":"38","author":"Duan","year":"2020","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0755","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1126\/science.abd3072","article-title":"Neuropilin-1 is a host factor for SARS-CoV-2 infection","volume":"370","author":"Daly","year":"2020","journal-title":"Science (80-.)"},{"key":"10.1016\/j.bcp.2022.115335_b0760","doi-asserted-by":"crossref","first-page":"1856","DOI":"10.1038\/s41598-022-05968-4","article-title":"Galectin-3 as a potential prognostic biomarker of severe COVID-19 in SARS-CoV-2 infected patients","volume":"12","author":"Cervantes-Alvarez","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2022.115335_b0765","doi-asserted-by":"crossref","first-page":"7215","DOI":"10.1128\/mBio.00384-21","article-title":"Galectin-9, a player in cytokine release syndrome and a surrogate diagnostic biomarker in SARS-CoV-2 infection","volume":"12","author":"Bozorgmehr","year":"2021","journal-title":"MBio"},{"key":"10.1016\/j.bcp.2022.115335_b0770","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.4049\/jimmunol.165.4.2156","article-title":"Human galectin-3 is a novel chemoattractant for monocytes and macrophages","volume":"165","author":"Sano","year":"2000","journal-title":"J. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0775","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1161\/JAHA.113.000263","article-title":"Heterogenic endothelial responses to inflammation: role for differential N-glycosylation and vascular bed of origin","volume":"2","author":"Scott","year":"2013","journal-title":"J. Am. Heart Assoc."},{"key":"10.1016\/j.bcp.2022.115335_b0780","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-020-71748-7","article-title":"Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition","volume":"10","author":"Grant","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2022.115335_b0785","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13601-015-0086-3","article-title":"Expression profiling and functional analysis of Toll-like receptors in primary healthy human nasal epithelial cells shows no correlation and a refractory LPS response","volume":"5","author":"Van Tongeren","year":"2015","journal-title":"Clin. Transl. Allergy"},{"key":"10.1016\/j.bcp.2022.115335_b0790","first-page":"694","article-title":"Interactions between TLR2, TLR4, and mannose receptors with gp43 from Paracoccidioides brasiliensis induce cytokine production by human monocytes","volume":"49","author":"Nakaira-Takahagi","year":"2011","journal-title":"Med. Mycol."},{"key":"10.1016\/j.bcp.2022.115335_b0795","doi-asserted-by":"crossref","unstructured":"D. Perez-zsolt, J. Mu\u00f1oz-basagoiti, J. Rodon, M. Elousa, D. Ra\u00efch-, Siglec-1 on dendritic cells mediates SARS- CoV-2 trans -infection of target cells while on macrophages triggers proinflammatory responses, (2021) 443572, doi: 10.1101\/2021.05.11.443572.","DOI":"10.1101\/2021.05.11.443572"},{"key":"10.1016\/j.bcp.2022.115335_b0800","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2020.01708","article-title":"Cytokine storm in COVID-19: the current evidence and treatment strategies","volume":"11","author":"Tang","year":"2020","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bcp.2022.115335_b0805","doi-asserted-by":"crossref","unstructured":"V.J. Costela-ruiz, R. Illescas-montes, J.M. Puerta-puerta, C. Ruiz, L. Melguizo-rodr\u00edguez, SARS-CoV-2 infection: the role of cytokines in COVID-19 disease, Cytokine Growth Factor Rev. 54 (2020) 62\u201375.","DOI":"10.1016\/j.cytogfr.2020.06.001"}],"container-title":["Biochemical Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295222004294?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295222004294?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T13:48:08Z","timestamp":1757771288000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006295222004294"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12]]},"references-count":161,"alternative-id":["S0006295222004294"],"URL":"https:\/\/doi.org\/10.1016\/j.bcp.2022.115335","relation":{},"ISSN":["0006-2952"],"issn-type":[{"value":"0006-2952","type":"print"}],"subject":[],"published":{"date-parts":[[2022,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glycosylation in SARS-CoV-2 variants: A path to infection and recovery","name":"articletitle","label":"Article Title"},{"value":"Biochemical Pharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bcp.2022.115335","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115335"}}