dc.contributor.author | Go, Eden P. | |
dc.contributor.author | Zhang, Ying | |
dc.contributor.author | Menon, Sushma | |
dc.contributor.author | Desaire, Heather | |
dc.date.accessioned | 2017-05-05T16:59:29Z | |
dc.date.available | 2017-05-05T16:59:29Z | |
dc.date.issued | 2011-02-04 | |
dc.identifier.citation | Go, E. P., Zhang, Y., Menon, S., & Desaire, H. (2011). Analysis of the disulfide bond arrangement of the HIV envelope protein CON-S gp140 ΔCFI shows variability in the V1 and V2 regions. Journal of Proteome Research, 10(2), 578–591. http://doi.org/10.1021/pr100764a | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23906 | |
dc.description.abstract | Disulfide bonding of cysteines is one of the most important protein modifications, and it plays a key role in establishing/maintaining protein structures in biologically active forms. Therefore, the determination of disulfide bond arrangement is one important aspect to understanding the chemical structure of a protein and defining its functional domains. Herein, aiming to understand how the HIV-1 envelope protein’s structure influences its immunogenicity, we used an MS-based
approach, liquid chromatography electrospray ionization Fourier transform ion cyclotron resonance (LC/ESI-FTICR) mass spectrometry, to determine the disulfide linkages on an oligomeric form of the group M consensus HIV-1 envelope protein (Env), CON-S gp140 ΔCFI. This protein has marked improvement in its immunogenicity, compared to monomeric gp120 and
wild-type forms of gp140 Envs. Our results demonstrate that the disulfide connectivity in the Nterminal region of CON-S gp140 ΔCFI is different from the disulfide bonding previously reported in the monomeric form of gp120 HIV-1 Env. Additionally, heterogeneity of the disulfide bonding was detected in this region. These data suggest that the V1/V2 region does not have a single, conserved disulfide bonding pattern, and that variability could impact immunogenicity of expressed Envs. | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | This document is the Accepted Manuscript version of a Published Work that appeared in final form in the Journal of Proteome Research, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/pr100764a. | en_US |
dc.subject | Disulfide | en_US |
dc.subject | Mass spectrometry | en_US |
dc.subject | HIV-1 | en_US |
dc.subject | Envelope protein | en_US |
dc.subject | LC/ESI-FTICR MS | en_US |
dc.title | Analysis of the disulfide bond arrangement of the HIV envelope protein CON-S gp140 ΔCFI shows variability in the V1 and V2 regions | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Go, Eden P. | |
kusw.kuauthor | Zhang, Ying | |
kusw.kuauthor | Menon, Sushma | |
kusw.kuauthor | Desaire, Heather | |
kusw.kudepartment | Chemistry | en_US |
dc.identifier.doi | 10.1021/pr100764a | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3075074 | en_US |
dc.rights.accessrights | openAccess | |