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High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection.

Publication ,  Journal Article
Lavine, CL; Lao, S; Montefiori, DC; Haynes, BF; Sodroski, JG; Yang, X; NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI),
Published in: J Virol
February 2012

Broad and potent neutralizing antibody (BNAb) responses are rare in people infected by human immunodeficiency virus type 1 (HIV-1). Clearly defining the nature of BNAb epitopes on HIV-1 envelope glycoproteins (Envs) targeted in vivo is critical for future directions of anti-HIV-1 vaccine development. Conventional techniques are successful in defining neutralizing epitopes in a small number of individual subjects but fail in studying large groups of subjects. Two independent methods were employed to investigate the nature of NAb epitopes targeted in 9 subjects, identified by the NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI) 001 and 008 clinical teams, known to make a strong BNAb response. Neutralizing activity from 8/9 subjects was enhanced by enriching high-mannose N-linked glycan (HM-glycan) of HIV-1 glycoproteins on neutralization target viruses and was sensitive to specific glycan deletion mutations of HIV-1 glycoproteins, indicating that HM-glycan-dependent epitopes are targeted by BNAb responses in these subjects. This discovery adds to accumulating evidence supporting the hypothesis that glycans are important targets on HIV-1 glycoproteins for BNAb responses in vivo, providing an important lead for future directions in developing NAb-based anti-HIV-1 vaccines.

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Published In

J Virol

DOI

EISSN

1098-5514

Publication Date

February 2012

Volume

86

Issue

4

Start / End Page

2153 / 2164

Location

United States

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Virology
  • Polysaccharides
  • Neutralization Tests
  • Mannose
  • Humans
  • HIV-1
  • HIV Infections
  • HIV Antibodies
  • Epitopes
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Lavine, C. L., Lao, S., Montefiori, D. C., Haynes, B. F., Sodroski, J. G., Yang, X., & NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI), . (2012). High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection. J Virol, 86(4), 2153–2164. https://doi.org/10.1128/JVI.06201-11
Lavine, Christy L., Socheata Lao, David C. Montefiori, Barton F. Haynes, Joseph G. Sodroski, Xinzhen Yang, and Xinzhen NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI). “High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection.J Virol 86, no. 4 (February 2012): 2153–64. https://doi.org/10.1128/JVI.06201-11.
Lavine CL, Lao S, Montefiori DC, Haynes BF, Sodroski JG, Yang X, et al. High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection. J Virol. 2012 Feb;86(4):2153–64.
Lavine, Christy L., et al. “High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection.J Virol, vol. 86, no. 4, Feb. 2012, pp. 2153–64. Pubmed, doi:10.1128/JVI.06201-11.
Lavine CL, Lao S, Montefiori DC, Haynes BF, Sodroski JG, Yang X, NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI). High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection. J Virol. 2012 Feb;86(4):2153–2164.

Published In

J Virol

DOI

EISSN

1098-5514

Publication Date

February 2012

Volume

86

Issue

4

Start / End Page

2153 / 2164

Location

United States

Related Subject Headings

  • env Gene Products, Human Immunodeficiency Virus
  • Virology
  • Polysaccharides
  • Neutralization Tests
  • Mannose
  • Humans
  • HIV-1
  • HIV Infections
  • HIV Antibodies
  • Epitopes