Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
Antibodies hedge their bets Most antibodies are highly specific, binding with high affinity to a single foreign antigen. However, an analysis of human immunodeficiency virus (HIV) envelope glycoprotein-specific monoclonal antibodies from infected subjects provides evidence for a surprisingly high de...
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| Published in | Nature (London) Vol. 467; no. 7315; pp. 591 - 595 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
30.09.2010
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0028-0836 1476-4687 1476-4687 |
| DOI | 10.1038/nature09385 |
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| Abstract | Antibodies hedge their bets
Most antibodies are highly specific, binding with high affinity to a single foreign antigen. However, an analysis of human immunodeficiency virus (HIV) envelope glycoprotein-specific monoclonal antibodies from infected subjects provides evidence for a surprisingly high degree of polyreactivity. Of 134 different antibodies directed at the gp140 envelope glycoprotein cloned from six patients, 75% were polyreactive, binding with high affinity to one gp140 site and with lower affinity to other sites on the viral surface. Relatively few gp140 glycoprotein spikes are displayed on the surface of HIV, so homotypic bivalent antibody binding is disfavoured and 'heteroligation' may help to improve net antibody affinity in such instances.
During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. Here, the monoclonal antibodies produced in two infected subjects in response to human immunodeficiency virus (HIV) glycoprotein have been analysed. The results provide evidence for polyreactivity, which may be required when the density of glycoprotein spikes is so low that bivalent binding is unlikely.
During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding
1
,
2
,
3
. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development
4
, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients
5
with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. |
|---|---|
| AbstractList | During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV disfavours homotypic bivalent antibody binding 1 – 3 . Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development 4 , it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients 5 with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naïve and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. [PUBLICATION ABSTRACT] Antibodies hedge their bets Most antibodies are highly specific, binding with high affinity to a single foreign antigen. However, an analysis of human immunodeficiency virus (HIV) envelope glycoprotein-specific monoclonal antibodies from infected subjects provides evidence for a surprisingly high degree of polyreactivity. Of 134 different antibodies directed at the gp140 envelope glycoprotein cloned from six patients, 75% were polyreactive, binding with high affinity to one gp140 site and with lower affinity to other sites on the viral surface. Relatively few gp140 glycoprotein spikes are displayed on the surface of HIV, so homotypic bivalent antibody binding is disfavoured and 'heteroligation' may help to improve net antibody affinity in such instances. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. Here, the monoclonal antibodies produced in two infected subjects in response to human immunodeficiency virus (HIV) glycoprotein have been analysed. The results provide evidence for polyreactivity, which may be required when the density of glycoprotein spikes is so low that bivalent binding is unlikely. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding 1 , 2 , 3 . Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development 4 , it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients 5 with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV.During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding. Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development, it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo homotypic bivalent binding. However, this type of binding is not always possible. For example, the small number of gp140 glycoprotein spikes displayed on the surface of the human immunodeficiency virus (HIV) disfavours homotypic bivalent antibody binding (1-3). Here we show that during the human antibody response to HIV, somatic mutations that increase antibody affinity also increase breadth and neutralizing potency. Surprisingly, the responding naive and memory B cells produce polyreactive antibodies, which are capable of bivalent heteroligation between one high-affinity anti-HIV-gp140 combining site and a second low-affinity site on another molecular structure on HIV. Although cross-reactivity to self-antigens or polyreactivity is strongly selected against during B-cell development (4), it is a common serologic feature of certain infections in humans, including HIV, Epstein-Barr virus and hepatitis C virus. Seventy-five per cent of the 134 monoclonal anti-HIV-gp140 antibodies cloned from six patients (5) with high titres of neutralizing antibodies are polyreactive. Despite the low affinity of the polyreactive combining site, heteroligation demonstrably increases the apparent affinity of polyreactive antibodies to HIV. |
| Audience | Academic |
| Author | Nussenzweig, Michel C. Artyomov, Maxim N. Mouquet, Hugo Wilson, Patrick C. Hope, Thomas J. Connors, Mark Ravetch, Jeffrey V. Scheid, Johannes F. Ott, Rene G. Zoller, Markus J. Walker, Bruce D. Seaman, Michael S. Chakraborty, Arup K. Eisen, Herman N. Shukair, Shetha Krogsgaard, Michelle Ho, David D. Pereyra, Florencia Pietzsch, John Wardemann, Hedda |
| AuthorAffiliation | 11 Aaron Diamond AIDS Research Center, New York, New York 10016, USA 10 Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School, Boston, Massachusetts 02114, USA 8 Institute of Chemistry and Biochemistry, Freie Universität Berlin, D 14195 Berlin, Germany 12 Section of Rheumatology, The Department of Medicine, University of Chicago, Chicago, Illinois 60637, USA 2 Charite Universitaetsmedizin, D-10117 Berlin, Germany 9 Laboratory of Immunoregulation, and Vaccine Research Center, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA 14 Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10065, USA 4 Department of Pathology and New York University Cancer Institute, New York University School of Medicine, New York, New York 10016, USA 7 Departments of Chemistry, Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integra |
| AuthorAffiliation_xml | – name: 7 Departments of Chemistry, Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA – name: 6 Department of Cell and Molecular Biology, Northwestern University, Chicago, Illinois 60611, USA – name: 10 Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School, Boston, Massachusetts 02114, USA – name: 1 Laboratory of Molecular Immunology, The Rockefeller University, New York, New York 10065, USA – name: 14 Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10065, USA – name: 13 Beth Israel Deaconess Medical Center. Boston, Massachusetts 02215, USA – name: 3 Max Planck Institute for Infection Biology, D-10117 Berlin, Germany – name: 4 Department of Pathology and New York University Cancer Institute, New York University School of Medicine, New York, New York 10016, USA – name: 9 Laboratory of Immunoregulation, and Vaccine Research Center, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA – name: 8 Institute of Chemistry and Biochemistry, Freie Universität Berlin, D 14195 Berlin, Germany – name: 12 Section of Rheumatology, The Department of Medicine, University of Chicago, Chicago, Illinois 60637, USA – name: 5 Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, New York 10065, USA – name: 11 Aaron Diamond AIDS Research Center, New York, New York 10016, USA – name: 2 Charite Universitaetsmedizin, D-10117 Berlin, Germany |
| Author_xml | – sequence: 1 givenname: Hugo surname: Mouquet fullname: Mouquet, Hugo organization: Laboratory of Molecular Immunology, The Rockefeller University – sequence: 2 givenname: Johannes F. surname: Scheid fullname: Scheid, Johannes F. organization: Laboratory of Molecular Immunology, The Rockefeller University, Charite Universitaetsmedizin – sequence: 3 givenname: Markus J. surname: Zoller fullname: Zoller, Markus J. organization: Max Planck Institute for Infection Biology – sequence: 4 givenname: Michelle surname: Krogsgaard fullname: Krogsgaard, Michelle organization: Department of Pathology and New York University Cancer Institute, New York University School of Medicine – sequence: 5 givenname: Rene G. surname: Ott fullname: Ott, Rene G. organization: Laboratory of Molecular Genetics and Immunology, The Rockefeller University – sequence: 6 givenname: Shetha surname: Shukair fullname: Shukair, Shetha organization: Department of Cell and Molecular Biology, Northwestern University – sequence: 7 givenname: Maxim N. surname: Artyomov fullname: Artyomov, Maxim N. organization: Departments of Chemistry, Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology – sequence: 8 givenname: John surname: Pietzsch fullname: Pietzsch, John organization: Laboratory of Molecular Immunology, The Rockefeller University, Institute of Chemistry and Biochemistry, Freie Universität Berlin – sequence: 9 givenname: Mark surname: Connors fullname: Connors, Mark organization: Laboratory of Immunoregulation, and Vaccine Research Center, National Institutes of Allergy and Infectious Diseases, National Institutes of Health – sequence: 10 givenname: Florencia surname: Pereyra fullname: Pereyra, Florencia organization: Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School – sequence: 11 givenname: Bruce D. surname: Walker fullname: Walker, Bruce D. organization: Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School – sequence: 12 givenname: David D. surname: Ho fullname: Ho, David D. organization: Aaron Diamond AIDS Research Center – sequence: 13 givenname: Patrick C. surname: Wilson fullname: Wilson, Patrick C. organization: The Department of Medicine, Section of Rheumatology, University of Chicago – sequence: 14 givenname: Michael S. surname: Seaman fullname: Seaman, Michael S. organization: Beth Israel Deaconess Medical Center – sequence: 15 givenname: Herman N. surname: Eisen fullname: Eisen, Herman N. organization: Departments of Chemistry, Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology – sequence: 16 givenname: Arup K. surname: Chakraborty fullname: Chakraborty, Arup K. organization: Departments of Chemistry, Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology – sequence: 17 givenname: Thomas J. surname: Hope fullname: Hope, Thomas J. organization: Department of Cell and Molecular Biology, Northwestern University – sequence: 18 givenname: Jeffrey V. surname: Ravetch fullname: Ravetch, Jeffrey V. organization: Laboratory of Molecular Genetics and Immunology, The Rockefeller University – sequence: 19 givenname: Hedda surname: Wardemann fullname: Wardemann, Hedda organization: Max Planck Institute for Infection Biology – sequence: 20 givenname: Michel C. surname: Nussenzweig fullname: Nussenzweig, Michel C. email: nussenzweig@rockefeller.edu organization: Laboratory of Molecular Immunology, The Rockefeller University, Howard Hughes Medical Institute, The Rockefeller University |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23248359$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/20882016$$D View this record in MEDLINE/PubMed |
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| Snippet | Antibodies hedge their bets
Most antibodies are highly specific, binding with high affinity to a single foreign antigen. However, an analysis of human... During immune responses, antibodies are selected for their ability to bind to foreign antigens with high affinity, in part by their ability to undergo... |
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| SubjectTerms | 631/250/2152/2153/1291 631/250/249/1570/1901 631/326/596/2553 Antibodies Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antibody Affinity - genetics Antibody Affinity - immunology Antigen-Antibody Reactions - genetics Antigen-Antibody Reactions - immunology Binding sites Biochemistry Biological and medical sciences Cardiolipins - immunology Cell Line, Tumor Chemical properties Competition Cross Reactions - genetics Cross Reactions - immunology env Gene Products, Human Immunodeficiency Virus - immunology Enzyme-Linked Immunosorbent Assay Epitopes - chemistry Epitopes - immunology Epstein-Barr virus Experiments Fundamental and applied biological sciences. Psychology Hepatitis C virus HIV (Viruses) HIV Antibodies - genetics HIV Antibodies - immunology HIV Antigens - chemistry HIV Antigens - immunology HIV-1 - chemistry HIV-1 - immunology Human immunodeficiency virus Humanities and Social Sciences Humans Immune response Immunoglobulin Fab Fragments - genetics Immunoglobulin Fab Fragments - immunology Immunoglobulin Heavy Chains - genetics Immunoglobulin Heavy Chains - immunology Immunology letter Microbiology Miscellaneous multidisciplinary Mutation Reactivity (Chemistry) Science Science (multidisciplinary) Surface Plasmon Resonance Viral antibodies Virology |
| Title | Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation |
| URI | https://link.springer.com/article/10.1038/nature09385 https://www.ncbi.nlm.nih.gov/pubmed/20882016 https://www.proquest.com/docview/763129020 https://www.proquest.com/docview/756299363 https://www.proquest.com/docview/902347560 https://pubmed.ncbi.nlm.nih.gov/PMC3699875 |
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