Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth
Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibod...
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| Published in | Immunity (Cambridge, Mass.) Vol. 45; no. 5; pp. 1108 - 1121 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
15.11.2016
Elsevier Limited |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis.
•CD4bs antibody N6 potently neutralizes 98% of HIV isolates•N6 potently neutralizes isolates resistant to other CD4bs antibodies•N6 evolved from an early intermediate within a VRC01-class antibody lineage•Unique structural features circumvent mechanisms of resistance to the VRC01 class
Detailed studies of broadly neutralizing antibodies are providing important information for the development of therapies, prophylaxis, and vaccines for HIV-1. Huang et al. report a CD4-binding-site antibody that evolved to circumvent common mechanisms of resistance, resulting in an antibody that achieves potent, near-pan neutralization of HIV-1. |
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| AbstractList | Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis.
•CD4bs antibody N6 potently neutralizes 98% of HIV isolates•N6 potently neutralizes isolates resistant to other CD4bs antibodies•N6 evolved from an early intermediate within a VRC01-class antibody lineage•Unique structural features circumvent mechanisms of resistance to the VRC01 class
Detailed studies of broadly neutralizing antibodies are providing important information for the development of therapies, prophylaxis, and vaccines for HIV-1. Huang et al. report a CD4-binding-site antibody that evolved to circumvent common mechanisms of resistance, resulting in an antibody that achieves potent, near-pan neutralization of HIV-1. Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis. Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis. Detailed studies of broadly neutralizing antibodies are providing important information for the development of therapies, prophylaxis, and vaccines for HIV-1. Huang et al. report a CD4-binding-site antibody that evolved to circumvent common mechanisms of resistance, resulting in an antibody that achieves potent, near-pan neutralization of HIV-1. Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis. Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis.Detailed studies of the broadly neutralizing antibodies (bNAbs) that underlie the best available examples of the humoral immune response to HIV are providing important information for the development of therapies and prophylaxis for HIV-1 infection. Here, we report a CD4-binding site (CD4bs) antibody, named N6, that potently neutralized 98% of HIV-1 isolates, including 16 of 20 that were resistant to other members of its class. N6 evolved a mode of recognition such that its binding was not impacted by the loss of individual contacts across the immunoglobulin heavy chain. In addition, structural analysis revealed that the orientation of N6 permitted it to avoid steric clashes with glycans, which is a common mechanism of resistance. Thus, an HIV-1-specific bNAb can achieve potent, near-pan neutralization of HIV-1, making it an attractive candidate for use in therapy and prophylaxis. |
| Author | Migueles, Stephen A. Zhang, Baoshan Douek, Daniel C. Parks, Robert Joyce, M. Gordon Darko, Sam Connors, Mark Kelsoe, Garnett Louder, Mark K. Von Holle, Tarra Kwong, Peter D. Huang, Jinghe Griesman, Trevor Asokan, Mangaiarkarasi Kang, Byong H. McKee, Krisha Sheng, Zizhang Alam, S. Munir Druz, Aliaksandr Georgiev, Ivelin S. Wu, Fan O’Dell, Sijy Bailer, Robert T. Ransier, Amy Mascola, John R. Haynes, Barton F. Chuang, Gwo-Yu Ishida, Elise Doria-Rose, Nicole A. Zhou, Tongqing Seaman, Michael S. Schramm, Chaim A. Hirsch, Vanessa Shapiro, Lawrence Zheng, Anqi |
| AuthorAffiliation | 3 Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA 5 Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA 7 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA 4 Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA 1 HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA 2 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA 6 Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA |
| AuthorAffiliation_xml | – name: 1 HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – name: 2 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – name: 3 Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – name: 7 Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA – name: 4 Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA – name: 5 Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA – name: 6 Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA |
| Author_xml | – sequence: 1 givenname: Jinghe surname: Huang fullname: Huang, Jinghe organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 2 givenname: Byong H. surname: Kang fullname: Kang, Byong H. organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 3 givenname: Elise surname: Ishida fullname: Ishida, Elise organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 4 givenname: Tongqing surname: Zhou fullname: Zhou, Tongqing organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 5 givenname: Trevor surname: Griesman fullname: Griesman, Trevor organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 6 givenname: Zizhang surname: Sheng fullname: Sheng, Zizhang organization: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA – sequence: 7 givenname: Fan surname: Wu fullname: Wu, Fan organization: Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 8 givenname: Nicole A. surname: Doria-Rose fullname: Doria-Rose, Nicole A. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 9 givenname: Baoshan surname: Zhang fullname: Zhang, Baoshan organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 10 givenname: Krisha surname: McKee fullname: McKee, Krisha organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 11 givenname: Sijy surname: O’Dell fullname: O’Dell, Sijy organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 12 givenname: Gwo-Yu surname: Chuang fullname: Chuang, Gwo-Yu organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 13 givenname: Aliaksandr surname: Druz fullname: Druz, Aliaksandr organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 14 givenname: Ivelin S. surname: Georgiev fullname: Georgiev, Ivelin S. organization: Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA – sequence: 15 givenname: Chaim A. surname: Schramm fullname: Schramm, Chaim A. organization: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA – sequence: 16 givenname: Anqi surname: Zheng fullname: Zheng, Anqi organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 17 givenname: M. Gordon surname: Joyce fullname: Joyce, M. Gordon organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 18 givenname: Mangaiarkarasi surname: Asokan fullname: Asokan, Mangaiarkarasi organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 19 givenname: Amy surname: Ransier fullname: Ransier, Amy organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 20 givenname: Sam surname: Darko fullname: Darko, Sam organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 21 givenname: Stephen A. surname: Migueles fullname: Migueles, Stephen A. organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 22 givenname: Robert T. surname: Bailer fullname: Bailer, Robert T. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 23 givenname: Mark K. surname: Louder fullname: Louder, Mark K. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 24 givenname: S. Munir surname: Alam fullname: Alam, S. Munir organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 25 givenname: Robert surname: Parks fullname: Parks, Robert organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 26 givenname: Garnett surname: Kelsoe fullname: Kelsoe, Garnett organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 27 givenname: Tarra surname: Von Holle fullname: Von Holle, Tarra organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 28 givenname: Barton F. surname: Haynes fullname: Haynes, Barton F. organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 29 givenname: Daniel C. surname: Douek fullname: Douek, Daniel C. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 30 givenname: Vanessa surname: Hirsch fullname: Hirsch, Vanessa organization: Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 31 givenname: Michael S. surname: Seaman fullname: Seaman, Michael S. organization: Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA – sequence: 32 givenname: Lawrence surname: Shapiro fullname: Shapiro, Lawrence organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 33 givenname: John R. surname: Mascola fullname: Mascola, John R. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 34 givenname: Peter D. surname: Kwong fullname: Kwong, Peter D. organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA – sequence: 35 givenname: Mark surname: Connors fullname: Connors, Mark email: mconnors@nih.gov organization: HIV-Specific Immunity Section of the Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/27851912$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1338973$$D View this record in Osti.gov |
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| Title | Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth |
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