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    Glycosylation Site-Specific Analysis of Clade C HIV-1 Envelope Proteins

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    Go_2009.pdf (5.887Mb)
    Issue Date
    2009-09
    Author
    Go, Eden P.
    Chang, Qing
    Liao, Hua-Xin
    Sutherland, Laura L.
    Alam, S. Munir
    Haynes, Barton F.
    Desaire, Heather
    Publisher
    American Chemical Society
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
    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/pr9002728.
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    Abstract
    The extensive glycosylation of HIV-1 envelope proteins (Env), gp120/gp41, is known to play an important role in evasion of host immune response by masking key neutralization epitopes and presenting the Env glycosylation as “self” to the host immune system. The Env glycosylation is mostly conserved but continues to evolve to modulate viral infectivity. Thus, profiling Env glycosylation and distinguishing interclade and intraclade glycosylation variations are necessary components in unraveling the effects of glycosylation on Env’s immunogenicity. Here, we describe a mass spectrometry-based approach to characterize the glycosylation profiles of two rVV-expressed clade C Envs by identifying the glycan motifs on each glycosylation site and determining the degree of glycosylation site occupancy. One Env is a wild-type Env, while the other is a synthetic “consensus” sequence (C.CON). The observed differences in the glycosylation profiles between the two clade C Envs show that C.CON has more unutilized sites and high levels of high mannose glycans; these features mimic the glycosylation profile of a Group M consensus immunogen, CONS. Our results also reveal a clade-specific glycosylation pattern. Discerning interclade and intraclade glycosylation variations could provide valuable information in understanding the molecular differences among the different HIV-1 clades and in designing new Env-based immunogens.
    URI
    http://hdl.handle.net/1808/23908
    DOI
    https://doi.org/10.1021/pr9002728
    Collections
    • Chemistry Scholarly Works [626]
    Citation
    Go, E. P., Chang, Q., Liao, H.-X., Sutherland, L. L., Alam, S. M., Haynes, B. F., & Desaire, H. (2009). Glycosylation Site-Specific Analysis of Clade C HIV-1 Envelope Proteins. Journal of Proteome Research, 8(9), 4231–4242. http://doi.org/10.1021/pr9002728

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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