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Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry.

Publication ,  Journal Article
Go, EP; Hewawasam, G; Liao, H-X; Chen, H; Ping, L-H; Anderson, JA; Hua, DC; Haynes, BF; Desaire, H
Published in: J Virol
August 2011

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.

Duke Scholars

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Published In

J Virol

DOI

EISSN

1098-5514

Publication Date

August 2011

Volume

85

Issue

16

Start / End Page

8270 / 8284

Location

United States

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Virology
  • Trypsin
  • Sequence Alignment
  • Mass Spectrometry
  • Humans
  • HIV-1
  • HIV Infections
  • HEK293 Cells
  • Glycosylation
 

Citation

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Go, E. P., Hewawasam, G., Liao, H.-X., Chen, H., Ping, L.-H., Anderson, J. A., … Desaire, H. (2011). Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol, 85(16), 8270–8284. https://doi.org/10.1128/JVI.05053-11
Go, Eden P., Geetha Hewawasam, Hua-Xin Liao, Haiyan Chen, Li-Hua Ping, Jeffrey A. Anderson, David C. Hua, Barton F. Haynes, and Heather Desaire. “Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry.J Virol 85, no. 16 (August 2011): 8270–84. https://doi.org/10.1128/JVI.05053-11.
Go EP, Hewawasam G, Liao H-X, Chen H, Ping L-H, Anderson JA, et al. Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol. 2011 Aug;85(16):8270–84.
Go, Eden P., et al. “Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry.J Virol, vol. 85, no. 16, Aug. 2011, pp. 8270–84. Pubmed, doi:10.1128/JVI.05053-11.
Go EP, Hewawasam G, Liao H-X, Chen H, Ping L-H, Anderson JA, Hua DC, Haynes BF, Desaire H. Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol. 2011 Aug;85(16):8270–8284.

Published In

J Virol

DOI

EISSN

1098-5514

Publication Date

August 2011

Volume

85

Issue

16

Start / End Page

8270 / 8284

Location

United States

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Virology
  • Trypsin
  • Sequence Alignment
  • Mass Spectrometry
  • Humans
  • HIV-1
  • HIV Infections
  • HEK293 Cells
  • Glycosylation