dc.contributor.author | Go, Eden P. | |
dc.contributor.author | Hewawasam, Geetha S. | |
dc.contributor.author | Lio, Hua-Xin | |
dc.contributor.author | Chen, Haiyan | |
dc.contributor.author | Ping, Li-Hua | |
dc.contributor.author | Anderson, Jeffrey A. | |
dc.contributor.author | Hua, David C. | |
dc.contributor.author | Haynes, Barton F. | |
dc.contributor.author | Desaire, Heather | |
dc.date.accessioned | 2014-12-05T15:51:02Z | |
dc.date.available | 2014-12-05T15:51:02Z | |
dc.date.issued | 2011-08-01 | |
dc.identifier.citation | Go, 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.uri | http://hdl.handle.net/1808/16043 | |
dc.description | This is the published version, also available here: http://dx.doi.org/10.1128/JVI.05053-11. | |
dc.description.abstract | The 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.publisher | American Society for Microbiology | |
dc.title | Characterization of Glycosylation Profiles of HIV-1 Transmitted/Founder Envelopes by Mass Spectrometry | |
dc.type | Article | |
kusw.kuauthor | Go, Eden P. | |
kusw.kuauthor | Hewawasam, Geetha | |
kusw.kuauthor | Hua, David C. | |
kusw.kuauthor | Desaire, Heather | |
kusw.kudepartment | Chemistry | |
kusw.oastatus | fullparticipation | |
dc.identifier.doi | 10.1128/JVI.05053-11 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess | |