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dc.contributor.authorGo, Eden P.
dc.contributor.authorHewawasam, Geetha S.
dc.contributor.authorLio, Hua-Xin
dc.contributor.authorChen, Haiyan
dc.contributor.authorPing, Li-Hua
dc.contributor.authorAnderson, Jeffrey A.
dc.contributor.authorHua, David C.
dc.contributor.authorHaynes, Barton F.
dc.contributor.authorDesaire, Heather
dc.date.accessioned2014-12-05T15:51:02Z
dc.date.available2014-12-05T15:51:02Z
dc.date.issued2011-08-01
dc.identifier.citationGo, Eden P., Hewawasam, Geetha., Lio, Hua-Xin., Chen, Haiyan., Ping, Li-Hua., Anderson, Jeffrey A., Hua, David C., Haynes, Barton F., Desaire, Heather. "Characterization of Glycosylation Profiles of HIV-1 Transmitted/Founder Envelopes by Mass Spectrometry." J. Virol. August 2011 vol. 85 no. 16 8270-8284. http://dx.doi.org/10.1128/JVI.05053-11.
dc.identifier.urihttp://hdl.handle.net/1808/16043
dc.descriptionThis is the published version, also available here: http://dx.doi.org/10.1128/JVI.05053-11.
dc.description.abstractThe analysis of HIV-1 envelope carbohydrates is critical to understanding their roles in HIV-1 transmission as well as in binding of envelope to HIV-1 antibodies. However, direct analysis of protein glycosylation by glycopeptide-based mass mapping approaches involves structural simplification of proteins with the use of a protease followed by an isolation and/or enrichment step before mass analysis. The successful completion of glycosylation analysis is still a major analytical challenge due to the complexity of samples, wide dynamic range of glycopeptide concentrations, and glycosylation heterogeneity. Here, we use a novel experimental workflow that includes an up-front complete or partial enzymatic deglycosylation step before trypsin digestion to characterize the glycosylation patterns and maximize the glycosylation coverage of two recombinant HIV-1 transmitted/founder envelope oligomers derived from clade B and C viruses isolated from acute infection and expressed in 293T cells. Our results show that both transmitted/founder Envs had similar degrees of glycosylation site occupancy as well as similar glycan profiles. Compared to 293T-derived recombinant Envs from viruses isolated from chronic HIV-1, transmitted/founder Envs displayed marked differences in their glycosylation site occupancies and in their amounts of complex glycans. Our analysis reveals that the glycosylation patterns of transmitted/founder Envs from two different clades (B and C) are more similar to each other than they are to the glycosylation patterns of chronic HIV-1 Envs derived from their own clades.
dc.publisherAmerican Society for Microbiology
dc.titleCharacterization of Glycosylation Profiles of HIV-1 Transmitted/Founder Envelopes by Mass Spectrometry
dc.typeArticle
kusw.kuauthorGo, Eden P.
kusw.kuauthorHewawasam, Geetha
kusw.kuauthorHua, David C.
kusw.kuauthorDesaire, Heather
kusw.kudepartmentChemistry
kusw.oastatusfullparticipation
dc.identifier.doi10.1128/JVI.05053-11
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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