{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:17:00Z","timestamp":1792786620884,"version":"4.5.0"},"reference-count":30,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,10,1]],"date-time":"2016-10-01T00:00:00Z","timestamp":1475280000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Indresh Srivastava (NIH Vaccine Research Center)","id":[{"id":"https:\/\/ror.org\/02fve6a73","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Patrick McHugh and Jian He"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Chromatography B"],"published-print":{"date-parts":[[2016,10]]},"DOI":"10.1016\/j.jchromb.2016.04.025","type":"journal-article","created":{"date-parts":[[2016,4,30]],"date-time":"2016-04-30T20:02:23Z","timestamp":1462046543000},"page":"218-223","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"special_numbering":"C","title":["Characterization of N -glycosylation profiles from mammalian and insect cell derived chikungunya VLP"],"prefix":"10.1016","volume":"1032","author":[{"given":"Catherine","family":"Lancaster","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavlo","family":"Pristatsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Van M.","family":"Hoang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danilo R.","family":"Casimiro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard M.","family":"Schwartz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Rustandi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sha","family":"Ha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jchromb.2016.04.025_bib0005","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/nrmicro2368","article-title":"Biology and pathogenesis of chikungunya virus","volume":"8","author":"Schwartz","year":"2010","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0010","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1099\/vir.0.82858-0","article-title":"Changing patterns of chikungunya virus: re-emergence of a zoonotic arbovirus","volume":"88","author":"Powers","year":"2007","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0015","doi-asserted-by":"crossref","first-page":"e623","DOI":"10.1371\/journal.pntd.0000623","article-title":"Chikungunya: a potentially emerging epidemic?","volume":"4","author":"Thiboutot","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0020","doi-asserted-by":"crossref","first-page":"e1168","DOI":"10.1371\/journal.pone.0001168","article-title":"Two Chikungunya isolates from the outbreak of La Reunion (Indian Ocean) exhibit different patterns of infection in the mosquito, Aedes albopictus","volume":"2","author":"Vazeille","year":"2007","journal-title":"PLoS One"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0025","doi-asserted-by":"crossref","first-page":"e201","DOI":"10.1371\/journal.ppat.0030201","article-title":"A single mutation in Chikungunya virus affects vector specificity and epidemic potential","volume":"3","author":"Tsetsarkin","year":"2007","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0030","doi-asserted-by":"crossref","first-page":"e928","DOI":"10.1371\/journal.pntd.0000928","article-title":"A DNA vaccine against chikungunya virus is protective in mice and induces neutralizing antibodies in mice and nonhuman primates","volume":"5","author":"Mallilankaraman","year":"2011","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0035","doi-asserted-by":"crossref","first-page":"681","DOI":"10.4269\/ajtmh.2000.62.681","article-title":"Phase II safety and immunogenicity study of live chikungunya virus vaccine TSI-GSD-218","volume":"62","author":"Edelman","year":"2000","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0040","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002142","article-title":"Novel chikungunya vaccine candidate with an IRES-based attenuation and host range alteration mechanism","volume":"7","author":"Plante","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0045","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1038\/nm.2105","article-title":"A virus-like particle vaccine for epidemic Chikungunya virus protects nonhuman primates against infection","volume":"16","author":"Akahata","year":"2010","journal-title":"Nat. Med."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0050","doi-asserted-by":"crossref","first-page":"e2124","DOI":"10.1371\/journal.pntd.0002124","article-title":"Effective chikungunya virus-like particle vaccine produced in insect cells","volume":"7","author":"Metz","year":"2013","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0055","doi-asserted-by":"crossref","first-page":"4305","DOI":"10.1002\/jps.23749","article-title":"Development of a stable virus-like particle vaccine formulation against Chikungunya virus and investigation of the effects of polyanions","volume":"102","author":"Kramer","year":"2013","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0060","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.virusres.2012.05.004","article-title":"Subunit vaccine formulations based on recombinant envelop proteins of Chikungunya virus elicit balanced Th1\/Th2 response and virus-neutralizing antibodies in mice","volume":"167","author":"Khan","year":"2012","journal-title":"Virus Res."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0065","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1016\/S0140-6736(14)61185-5","article-title":"Safety and tolerability of chikungunya virus-like particle vaccine in healthy adults: a phase 1 dose-escalation trial","volume":"384","author":"Chang","year":"2014","journal-title":"Lancet"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0070","doi-asserted-by":"crossref","first-page":"220","DOI":"10.4049\/jimmunol.1201060","article-title":"Toward animal cell culture-based influenza vaccine design: viral hemagglutinin N-glycosylation markedly impacts immunogenicity","volume":"190","author":"H\u00fctter","year":"2013","journal-title":"J. Immunol."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0075","doi-asserted-by":"crossref","first-page":"e66719","DOI":"10.1371\/journal.pone.0066719","article-title":"Different immunity elicited by recombinant H5N1 hemagglutinin proteins containing pauci-mannose, high-mannose, or complex type N-glycans","volume":"8","author":"Lin","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0080","doi-asserted-by":"crossref","first-page":"3707","DOI":"10.1021\/pr400329k","article-title":"Comparative glycomics analysis of influenza hemagglutinin (H5N1) produced in vaccine relevant cell platforms","volume":"12","author":"An","year":"2013","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0085","doi-asserted-by":"crossref","first-page":"4325","DOI":"10.1016\/j.vaccine.2009.04.076","article-title":"Glycan analysis in cell culture-based influenza vaccine production: influence of host cell line and virus strain on the glycosylation pattern of viral hemagglutinin","volume":"27","author":"Schwarzer","year":"2009","journal-title":"Vaccine"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0090","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1002\/bit.24834","article-title":"Impact of cultivation conditions on N-glycosylation of influenza virus A hemagglutinin produed in MDCK cell culture","volume":"110","author":"R\u00f6dig","year":"2013","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0095","doi-asserted-by":"crossref","first-page":"13800","DOI":"10.1073\/pnas.1006498107","article-title":"Envelop glycans of immunodeficiency virions are almost entirely oligomannose antigens","volume":"107","author":"Doores","year":"2010","journal-title":"PNAS"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0100","doi-asserted-by":"crossref","first-page":"e23521","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.jchromb.2016.04.025_bib0105","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/nature09555","article-title":"Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography","volume":"468","author":"Voss","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0110","doi-asserted-by":"crossref","first-page":"2548","DOI":"10.1016\/S0021-9258(18)32961-2","article-title":"Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins","volume":"258","author":"Hsieh","year":"1983","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0115","doi-asserted-by":"crossref","first-page":"19303","DOI":"10.1016\/S0021-9258(19)77635-2","article-title":"Regulation of glycosylation: the influence of protein structure on N-linked oligosaccharide processing","volume":"263","author":"Hubbard","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0120","doi-asserted-by":"crossref","first-page":"2375","DOI":"10.1016\/S0021-9258(17)43362-X","article-title":"Regulation of asparagine-linked oligosaccharide processing Oligosaccharide processing in Aedes albopictus mosquito cells","volume":"259","author":"Hsieh","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0125","doi-asserted-by":"crossref","first-page":"e94401","DOI":"10.1371\/journal.pone.0094401","article-title":"Enhanced production of Chikungunya virus-like particles using a high-pH adapted Spodoptera fugiperda insect cell line","volume":"9","author":"Wagner","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0130","doi-asserted-by":"crossref","first-page":"2668","DOI":"10.1021\/cr3003714","article-title":"High-sensitivity analytical approaches for the structural characterization of glycoproteins","volume":"113","author":"Alley","year":"2013","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0135","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.chroma.2014.05.087","article-title":"Development and application of a reversed-phase high-performance liquid chromatographic method for quantitation and characterization of a Chikungunya virus-like particle vaccine","volume":"1364","author":"Shytuhina","year":"2014","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jchromb.2016.04.025_bib0140","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1002\/emmm.201200213","article-title":"Early neutralizing IgG response to Chikungunya virus in infected patients targets a dominant linear epitope on the E2 glycoprotein","volume":"4","author":"Kam","year":"2012","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0145","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002390","article-title":"Chikungunya virus neutralization antigens and direct cell-to-cell transmission are revealed by human antibody-escape mutants","volume":"7","author":"Lee","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jchromb.2016.04.025_bib0150","doi-asserted-by":"crossref","first-page":"e2423","DOI":"10.1371\/journal.pntd.0002423","article-title":"A neutralizing monoclonal antibody targeting the acid-sensitive region in chikungunya virus E2 protects from disease","volume":"7","author":"Selvarajah","year":"2013","journal-title":"PLoS Negl. Trop. Dis."}],"container-title":["Journal of Chromatography B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570023216302446?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570023216302446?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,6,19]],"date-time":"2022-06-19T08:55:54Z","timestamp":1655628954000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570023216302446"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,10]]},"references-count":30,"alternative-id":["S1570023216302446"],"URL":"https:\/\/doi.org\/10.1016\/j.jchromb.2016.04.025","relation":{},"ISSN":["1570-0232"],"issn-type":[{"value":"1570-0232","type":"print"}],"subject":[],"published":{"date-parts":[[2016,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Characterization of N-glycosylation profiles from mammalian and insect cell derived chikungunya VLP","name":"articletitle","label":"Article Title"},{"value":"Journal of Chromatography B","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jchromb.2016.04.025","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}