Show simple item record

dc.contributor.authorGo, Eden P.
dc.contributor.authorZhang, Ying
dc.contributor.authorMenon, Sushma
dc.contributor.authorDesaire, Heather
dc.date.accessioned2017-05-05T16:59:29Z
dc.date.available2017-05-05T16:59:29Z
dc.date.issued2011-02-04
dc.identifier.citationGo, 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/pr100764aen_US
dc.identifier.urihttp://hdl.handle.net/1808/23906
dc.description.abstractDisulfide 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.publisherAmerican Chemical Societyen_US
dc.rightsThis 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.subjectDisulfideen_US
dc.subjectMass spectrometryen_US
dc.subjectHIV-1en_US
dc.subjectEnvelope proteinen_US
dc.subjectLC/ESI-FTICR MSen_US
dc.titleAnalysis of the disulfide bond arrangement of the HIV envelope protein CON-S gp140 ΔCFI shows variability in the V1 and V2 regionsen_US
dc.typeArticleen_US
kusw.kuauthorGo, Eden P.
kusw.kuauthorZhang, Ying
kusw.kuauthorMenon, Sushma
kusw.kuauthorDesaire, Heather
kusw.kudepartmentChemistryen_US
dc.identifier.doi10.1021/pr100764aen_US
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC3075074en_US
dc.rights.accessrightsopenAccess


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record