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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
agricultural and biological sciences
Isolation of a monoclonal antibody that targets the alpha-2 helix of gp120 and represents the initial autologous neutralizing-antibody response in an HIV-1 subtype C-infected individual
Journal of Virology, Volume 85, No. 15, Year 2011
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Description
The C3-V4 region is a major target of autologous neutralizing antibodies in HIV-1 subtype C infection. We previously identified a Center for AIDS Program of Research in South Africa (CAPRISA) participant, CAP88, who developed a potent neutralizing-antibody response within 3 months of infection that targeted an epitope in the C3 region of the HIV-1 envelope (P. L. Moore et al., PLoS Pathog. 5:e1000598, 2009). Here we showed that these type-specific antibodies could be adsorbed using recombinant gp120 from the transmitted/founder virus from CAP88 but not by gp120 made from other isolates. Furthermore, this activity could be depleted using a chimeric gp120 protein that contained only the C3 region from the CAP88 viral envelope engrafted onto the unrelated CAP63 viral envelope (called 63-88C3). On the basis of this, a differential sorting of memory B cells was performed using gp120s made from 63-88C3 and CAP63 labeled with different fluorochromes as positive and negative probes, respectively. This strategy resulted in the isolation of a highly specific monoclonal antibody (MAb), called CAP88-CH06, that neutralized the CAP88 transmitted/founder virus and viruses from acute infection but was unable to neutralize CAP88 viruses isolated at 6 and 12 months postinfection. The latter viruses contained 2 amino acid changes in the alpha-2 helix of C3 that mediated escape from this MAb. One of these changes involved the introduction of an N-linked glycan at position 339 that occluded the epitope, while the other mutation (either E343K or E350K) was a charge change. Our data validate the use of differential sorting to isolate a MAb targeting a specific epitope in the envelope glycoprotein and provided insights into the mechanisms of autologous neutralization escape. © 2011, American Society for Microbiology.
Authors & Co-Authors
Gray, Elin Solomonovna
United States, Durham
Duke University School of Medicine
South Africa, Johannesburg
National Institute for Communicable Diseases
Moody, Michael Anthony
United States, Durham
Duke University School of Medicine
Wibmer, Constantinos Kurt
South Africa, Johannesburg
National Institute for Communicable Diseases
South Africa, Johannesburg
University of the Witwatersrand
Chen, Xi
United States, Durham
Duke University School of Medicine
Marshall, Dawn Jones
United States, Durham
Duke University School of Medicine
Amos, Joshua
United States, Durham
Duke University School of Medicine
Moore, Penny L.
South Africa, Johannesburg
National Institute for Communicable Diseases
South Africa, Johannesburg
University of the Witwatersrand
Foulger, Andrew
United States, Durham
Duke University School of Medicine
Yu, Jae Sung
United States, Durham
Duke University School of Medicine
Lambson, Bronwen E.
South Africa, Johannesburg
National Institute for Communicable Diseases
Abdool Karim, Salim S.
South Africa, Congella
Centre for the Aids Programme of Research in South Africa
Whitesides, John F.
United States, Durham
Duke University School of Medicine
Tomaras, Georgia D.
United States, Durham
Duke University School of Medicine
Haynes, Barton F.
United States, Durham
Duke University School of Medicine
Morris, Lynn
South Africa, Johannesburg
National Institute for Communicable Diseases
South Africa, Johannesburg
University of the Witwatersrand
Liao, Huaxin
United States, Durham
Duke University School of Medicine
Statistics
Citations: 62
Authors: 16
Affiliations: 4
Identifiers
Doi:
10.1128/JVI.00563-11
ISSN:
0022538X
e-ISSN:
10985514
Research Areas
Cancer
Infectious Diseases
Study Locations
South Africa