Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1

Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is v...

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Published inVirology (New York, N.Y.) Vol. 396; no. 2; pp. 339 - 348
Main Authors Nandi, Avishek, Lavine, Christine L., Wang, Pengcheng, Lipchina, Inna, Goepfert, Paul A., Shaw, George M., Tomaras, Georgia D., Montefiori, David C., Haynes, Barton F., Easterbrook, Philippa, Robinson, James E., Sodroski, Joseph G., Yang, Xinzhen
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 20.01.2010
Subjects
Antibodies, Neutralizing - immunology
CD4 Antigens - immunology
CD4BS
Envelope glycoprotein
Epitopes - immunology
Glycan
HIV Antibodies - immunology
HIV Antigens - immunology
HIV Envelope Protein gp120 - immunology
HIV Infections - immunology
HIV-1
HIV-1 - immunology
Human immunodeficiency virus 1
Humans
In vivo
Infectious Disease
Neutralization Tests
Neutralizing epitope
Recombinant Proteins - immunology
HIV-1
Neutralizing epitope
In vivo
CD4BS
V3
Envelope glycoprotein
Glycan
Online AccessGet full text
ISSN0042-6822
1096-0341
1096-0341
DOI10.1016/j.virol.2009.10.044

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Abstract Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved nonlinear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.
AbstractList Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved nonlinear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.
Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved non-linear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.
Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved nonlinear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved nonlinear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.
Abstract Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare cases, broad and potent nAbs are actually induced in vivo. Identifying specific epitopes targeted by such broad and potent nAb response is valuable in guiding the design of a prophylactic vaccine aimed to induce nAb. In this study, we have defined neutralizing epitope usage in 7 out of 17 subjects with broad and potent nAbs by using targeted mutagenesis in known neutralizing epitopes of HIV-1 glycoproteins and by using in vitro depletion of serum neutralizing activity by various recombinant HIV-1 glycoproteins. Consistent with recent reports, the CD4 binding site (CD4BS) is targeted by nAbs in vivo (4 of the 7 subjects with defined neutralizing epitopes). The new finding from this study is that epitopes in the gp120 outer domain are also targeted by nAbs in vivo (5 of the 7 subjects). The outer domain epitopes include glycan-dependent epitopes (2 subjects), conserved nonlinear epitope in the V3 region (2 subjects), and a CD4BS epitope composed mainly of the elements in the outer domain (1 subject). Importantly, we found indication for epitope poly-specificity, a dual usage of the V3 and CD4BS epitopes, in only one subject. This study provides a more complete profile of epitope usage for broad and potent nAb responses during HIV-1 infection.
Author Lavine, Christine L.
Nandi, Avishek
Sodroski, Joseph G.
Easterbrook, Philippa
Tomaras, Georgia D.
Lipchina, Inna
Yang, Xinzhen
Robinson, James E.
Shaw, George M.
Montefiori, David C.
Haynes, Barton F.
Wang, Pengcheng
Goepfert, Paul A.
AuthorAffiliation b Department of Medicine, University of Alabama School of Medicine, Birmingham, Alabama
f Department of Cancer Immunology & AIDS, Dana-Farber Cancer Institute, Department of Pathology, Division of AIDS, Boston, Massachusetts 02215
e Department of Pediatrics, Tulane University School of Medicine, New Orleans, Luisiana
d Department of HIV/GUM, King’s College, London, UK
a Division of Viral Pathogenesis, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215
c Duke Human Vaccine Institute, Duke University Medical Center, Raleigh, North Carolina
g Harvard Medical School, Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02215
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Issue 2
Keywords HIV-1
Neutralizing epitope
In vivo
CD4BS
V3
Envelope glycoprotein
Glycan
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elsevier_clinicalkey_doi_10_1016_j_virol_2009_10_044
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PublicationDate 2010-01-20
PublicationDateYYYYMMDD 2010-01-20
PublicationDate_xml – month: 01
  year: 2010
  text: 2010-01-20
  day: 20
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Virology (New York, N.Y.)
PublicationTitleAlternate Virology
PublicationYear 2010
Publisher Elsevier Inc
Publisher_xml – name: Elsevier Inc
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Snippet Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1 (HIV-1). In rare...
Abstract Neutralizing antibody (nAb) response is sporadic and has limited potency and breadth during infection with human immunodeficiency virus type 1...
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SubjectTerms Antibodies, Neutralizing - immunology
CD4 Antigens - immunology
CD4BS
Envelope glycoprotein
Epitopes - immunology
Glycan
HIV Antibodies - immunology
HIV Antigens - immunology
HIV Envelope Protein gp120 - immunology
HIV Infections - immunology
HIV-1
HIV-1 - immunology
Human immunodeficiency virus 1
Humans
In vivo
Infectious Disease
Neutralization Tests
Neutralizing epitope
Recombinant Proteins - immunology
Title Epitopes for broad and potent neutralizing antibody responses during chronic infection with human immunodeficiency virus type 1
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https://dx.doi.org/10.1016/j.virol.2009.10.044
https://www.ncbi.nlm.nih.gov/pubmed/19922969
https://www.proquest.com/docview/21162251
https://www.proquest.com/docview/734174219
https://pubmed.ncbi.nlm.nih.gov/PMC2789835
Volume 396
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