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Glycosylation site-specific analysis of clade C HIV-1 envelope proteins.

Publication ,  Journal Article
Go, EP; Chang, Q; Liao, H-X; Sutherland, LL; Alam, SM; Haynes, BF; Desaire, H
Published in: J Proteome Res
September 2009

The extensive glycosylation of HIV-1 envelope proteins (Envs), 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" Env (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, CON-S. 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.

Duke Scholars

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Published In

J Proteome Res

DOI

ISSN

1535-3893

Publication Date

September 2009

Volume

8

Issue

9

Start / End Page

4231 / 4242

Location

United States

Related Subject Headings

  • Sequence Alignment
  • Proteomics
  • Peptide Fragments
  • Molecular Sequence Data
  • Mass Spectrometry
  • Humans
  • HIV-1
  • HIV Envelope Protein gp41
  • HIV Envelope Protein gp120
  • Glycosylation
 

Citation

APA
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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. J Proteome Res, 8(9), 4231–4242. https://doi.org/10.1021/pr9002728
Go, Eden P., Qing Chang, Hua-Xin Liao, Laura L. Sutherland, S Munir Alam, Barton F. Haynes, and Heather Desaire. “Glycosylation site-specific analysis of clade C HIV-1 envelope proteins.J Proteome Res 8, no. 9 (September 2009): 4231–42. https://doi.org/10.1021/pr9002728.
Go EP, Chang Q, Liao H-X, Sutherland LL, Alam SM, Haynes BF, et al. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. J Proteome Res. 2009 Sep;8(9):4231–42.
Go, Eden P., et al. “Glycosylation site-specific analysis of clade C HIV-1 envelope proteins.J Proteome Res, vol. 8, no. 9, Sept. 2009, pp. 4231–42. Pubmed, doi:10.1021/pr9002728.
Go EP, Chang Q, Liao H-X, Sutherland LL, Alam SM, Haynes BF, Desaire H. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. J Proteome Res. 2009 Sep;8(9):4231–4242.
Journal cover image

Published In

J Proteome Res

DOI

ISSN

1535-3893

Publication Date

September 2009

Volume

8

Issue

9

Start / End Page

4231 / 4242

Location

United States

Related Subject Headings

  • Sequence Alignment
  • Proteomics
  • Peptide Fragments
  • Molecular Sequence Data
  • Mass Spectrometry
  • Humans
  • HIV-1
  • HIV Envelope Protein gp41
  • HIV Envelope Protein gp120
  • Glycosylation