Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1

Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structur...

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Published in	Science (American Association for the Advancement of Science) Vol. 329; no. 5993; pp. 856 - 861
Main Authors	Wu, Xueling, Yang, Zhi-Yong, Li, Yuxing, Hogerkorp, Carl-Magnus, Schief, William R, Seaman, Michael S, Zhou, Tongqing, Schmidt, Stephen D, Wu, Lan, Xu, Ling, Longo, Nancy S, McKee, Krisha, O'Dell, Sijy, Louder, Mark K, Wycuff, Diane L, Feng, Yu, Nason, Martha, Doria-Rose, Nicole, Connors, Mark, Kwong, Peter D, Roederer, Mario, Wyatt, Richard T, Nabel, Gary J, Mascola, John R
Format	Journal Article
Language	English
Published	United States American Association for the Advancement of Science 13.08.2010 The American Association for the Advancement of Science
Subjects	AIDS Vaccines Amino acids Antibodies Antibodies, Monoclonal - immunology Antibodies, Monoclonal - isolation & purification Antibodies, Neutralizing - immunology Antibodies, Neutralizing - isolation & purification Antibody Specificity B lymphocytes B-Lymphocytes - immunology Binding Binding Sites, Antibody CD4 Antigens - immunology CD4 Antigens - metabolism Circulating Cross Reactions Drug Design Envelopes Enzyme linked immunosorbent assay Epitopes - immunology Genes Genes, Immunoglobulin Heavy Chain Genes, Immunoglobulin Light Chain Glycoprotein Glycoproteins HIV HIV 1 HIV Antibodies - immunology HIV Antibodies - isolation & purification HIV Envelope Protein gp120 - chemistry HIV Envelope Protein gp120 - immunology HIV Envelope Protein gp120 - metabolism HIV infections HIV Infections - immunology HIV Infections - virology HIV-1 - genetics HIV-1 - immunology Human immunodeficiency virus Human immunodeficiency virus 1 Humans immunoglobulin genes Immunoglobulins Immunology Infectious diseases Molecular Sequence Data Monoclonal antibodies Neutralization Neutralization Tests Neutralizing neutralizing antibodies Protein Engineering Proteins Reactivity Recombinant Proteins - chemistry Recombinant Proteins - immunology Recombinant Proteins - metabolism Research facilities Vaccines Viruses
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Abstract	Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design.
AbstractList	Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design. Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologie basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design. Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design.Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design. Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1-infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design. [PUBLICATION ABSTRACT] Developing a protective HIV vaccine remains a top global health priority. One strategy to identify potential vaccine candidates is to isolate broadly neutralizing antibodies from infected individuals and then attempt to elicit the same antibody response through vaccination (see the Perspective by Burton and Weiss ). Wu et al. (p. 856 , published online 8 July) now report the identification of three broadly neutralizing antibodies, isolated from an HIV-1–infected individual, that exhibited great breadth and potency of neutralization and were specific for the co-receptor CD4-binding site of the glycoprotein 120 (gp120), part of the viral Env spike. Zhou et al. (p. 811 , published online 8 July) analyzed the crystal structure for one of these antibodies, VRC01, in complex with an HIV-1 gp120. VRC01 focuses its binding onto a conformationally invariant domain that is the site of initial CD4 attachment, which allows the antibody to overcome the glycan and conformational masking that diminishes the neutralization potency of most CD4-binding-site antibodies. The epitopes recognized by these antibodies suggest potential immunogens that can inform vaccine design. A human antibody achieves broad neutralization by binding the viral site of recognition for the primary host receptor, CD4. Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1–infected individuals, but the virologic basis of their neutralization remains poorly understood. We used knowledge of HIV-1 envelope structure to develop antigenically resurfaced glycoproteins specific for the structurally conserved site of initial CD4 receptor binding. These probes were used to identify sera with NAbs to the CD4-binding site (CD4bs) and to isolate individual B cells from such an HIV-1–infected donor. By expressing immunoglobulin genes from individual cells, we identified three monoclonal antibodies, including a pair of somatic variants that neutralized over 90% of circulating HIV-1 isolates. Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design.
Author	Kwong, Peter D Schief, William R Connors, Mark Nabel, Gary J Louder, Mark K Nason, Martha Wu, Lan Wyatt, Richard T Mascola, John R Roederer, Mario Schmidt, Stephen D Wu, Xueling Zhou, Tongqing Feng, Yu Doria-Rose, Nicole Li, Yuxing Hogerkorp, Carl-Magnus Longo, Nancy S McKee, Krisha O'Dell, Sijy Seaman, Michael S Xu, Ling Wycuff, Diane L Yang, Zhi-Yong
AuthorAffiliation	4 Department of Biochemistry, University of Washington, Seattle, WA 98195, USA 5 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA 2 Biostatistics Research Branch, Division of Clinical Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA 1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA 3 Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
AuthorAffiliation_xml	– name: 5 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA – name: 1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – name: 4 Department of Biochemistry, University of Washington, Seattle, WA 98195, USA – name: 2 Biostatistics Research Branch, Division of Clinical Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA – name: 3 Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Author_xml	– sequence: 1 fullname: Wu, Xueling – sequence: 2 fullname: Yang, Zhi-Yong – sequence: 3 fullname: Li, Yuxing – sequence: 4 fullname: Hogerkorp, Carl-Magnus – sequence: 5 fullname: Schief, William R – sequence: 6 fullname: Seaman, Michael S – sequence: 7 fullname: Zhou, Tongqing – sequence: 8 fullname: Schmidt, Stephen D – sequence: 9 fullname: Wu, Lan – sequence: 10 fullname: Xu, Ling – sequence: 11 fullname: Longo, Nancy S – sequence: 12 fullname: McKee, Krisha – sequence: 13 fullname: O'Dell, Sijy – sequence: 14 fullname: Louder, Mark K – sequence: 15 fullname: Wycuff, Diane L – sequence: 16 fullname: Feng, Yu – sequence: 17 fullname: Nason, Martha – sequence: 18 fullname: Doria-Rose, Nicole – sequence: 19 fullname: Connors, Mark – sequence: 20 fullname: Kwong, Peter D – sequence: 21 fullname: Roederer, Mario – sequence: 22 fullname: Wyatt, Richard T – sequence: 23 fullname: Nabel, Gary J – sequence: 24 fullname: Mascola, John R
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/20616233$$D View this record in MEDLINE/PubMed
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Snippet	Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologic basis of their neutralization remains... Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1-infected individuals, but the virologie basis of their neutralization remains... Developing a protective HIV vaccine remains a top global health priority. One strategy to identify potential vaccine candidates is to isolate broadly... Cross-reactive neutralizing antibodies (NAbs) are found in the sera of many HIV-1–infected individuals, but the virologic basis of their neutralization remains...
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SubjectTerms	AIDS Vaccines Amino acids Antibodies Antibodies, Monoclonal - immunology Antibodies, Monoclonal - isolation & purification Antibodies, Neutralizing - immunology Antibodies, Neutralizing - isolation & purification Antibody Specificity B lymphocytes B-Lymphocytes - immunology Binding Binding Sites, Antibody CD4 Antigens - immunology CD4 Antigens - metabolism Circulating Cross Reactions Drug Design Envelopes Enzyme linked immunosorbent assay Epitopes - immunology Genes Genes, Immunoglobulin Heavy Chain Genes, Immunoglobulin Light Chain Glycoprotein Glycoproteins HIV HIV 1 HIV Antibodies - immunology HIV Antibodies - isolation & purification HIV Envelope Protein gp120 - chemistry HIV Envelope Protein gp120 - immunology HIV Envelope Protein gp120 - metabolism HIV infections HIV Infections - immunology HIV Infections - virology HIV-1 - genetics HIV-1 - immunology Human immunodeficiency virus Human immunodeficiency virus 1 Humans immunoglobulin genes Immunoglobulins Immunology Infectious diseases Molecular Sequence Data Monoclonal antibodies Neutralization Neutralization Tests Neutralizing neutralizing antibodies Protein Engineering Proteins Reactivity Recombinant Proteins - chemistry Recombinant Proteins - immunology Recombinant Proteins - metabolism Research facilities Vaccines Viruses
Title	Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1
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