Human antibodies reveal a protective epitope that is highly conserved among human and nonhuman influenza A viruses
Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccin...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 107; no. 28; pp. 12658 - 12663 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
13.07.2010
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG⁺ memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. |
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| AbstractList | Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG⁺ memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG + memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG super(+) memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG + memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG(+) memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains.Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG(+) memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection. However, new viral strains emerge continuously because of the plasticity of the influenza genome, which necessitates annual reformulation of vaccine antigens, and resistance to antivirals can appear rapidly and become entrenched in circulating virus populations. In addition, the spread of new pandemic strains is difficult to contain because of the time required to engineer and manufacture effective vaccines. Monoclonal antibodies that target highly conserved viral epitopes might offer an alternative protection paradigm. Herein we describe the isolation of a panel of monoclonal antibodies derived from the IgG+ memory B cells of healthy, human subjects that recognize a previously unknown conformational epitope within the ectodomain of the influenza matrix 2 protein, M2e. This antibody binding region is highly conserved in influenza A viruses, being present in nearly all strains detected to date, including highly pathogenic viruses that infect primarily birds and swine, and the current 2009 swine-origin H1N1 pandemic strain (S-OIV). Furthermore, these human anti-M2e monoclonal antibodies protect mice from lethal challenges with either H5N1 or H1N1 influenza viruses. These results suggest that viral M2e can elicit broadly cross-reactive and protective antibodies in humans. Accordingly, recombinant forms of these human antibodies may provide useful therapeutic agents to protect against infection from a broad spectrum of influenza A strains. [PUBLICATION ABSTRACT] |
| Author | Hammond, Philip W. Grandea, Andres G. Mitcham, Jennifer L. Pekosz, Andrew Chisari, Francis V. Cox, Thomas C. Kiso, Maki Olsen, Ole A. Kawaoka, Yoshihiro Renshaw, Mark Hatta, Masato Chan-Hui, Po-Ying Stewart, Shaun M. Cieplak, Witold Grantham, Michael L. Moyle, Matthew Shinya, Kyoko |
| Author_xml | – sequence: 1 givenname: Andres G. surname: Grandea fullname: Grandea, Andres G. – sequence: 2 givenname: Ole A. surname: Olsen fullname: Olsen, Ole A. – sequence: 3 givenname: Thomas C. surname: Cox fullname: Cox, Thomas C. – sequence: 4 givenname: Mark surname: Renshaw fullname: Renshaw, Mark – sequence: 5 givenname: Philip W. surname: Hammond fullname: Hammond, Philip W. – sequence: 6 givenname: Po-Ying surname: Chan-Hui fullname: Chan-Hui, Po-Ying – sequence: 7 givenname: Jennifer L. surname: Mitcham fullname: Mitcham, Jennifer L. – sequence: 8 givenname: Witold surname: Cieplak fullname: Cieplak, Witold – sequence: 9 givenname: Shaun M. surname: Stewart fullname: Stewart, Shaun M. – sequence: 10 givenname: Michael L. surname: Grantham fullname: Grantham, Michael L. – sequence: 11 givenname: Andrew surname: Pekosz fullname: Pekosz, Andrew – sequence: 12 givenname: Maki surname: Kiso fullname: Kiso, Maki – sequence: 13 givenname: Kyoko surname: Shinya fullname: Shinya, Kyoko – sequence: 14 givenname: Masato surname: Hatta fullname: Hatta, Masato – sequence: 15 givenname: Yoshihiro surname: Kawaoka fullname: Kawaoka, Yoshihiro – sequence: 16 givenname: Matthew surname: Moyle fullname: Moyle, Matthew – sequence: 17 givenname: Francis V. surname: Chisari fullname: Chisari, Francis V. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20615945$$D View this record in MEDLINE/PubMed |
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| Copyright | copyright © 1993-2008 National Academy of Sciences of the United States of America Copyright National Academy of Sciences Jul 13, 2010 |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 Edited* by Francis V. Chisari, The Scripps Research Institute, La Jolla, CA, and approved June 1, 2010 (received for review October 12, 2009) Author contributions: A.G.G., O.A.O., J.L.M., W.C., A.P., Y.K., and M.M. designed research; A.G.G., T.C.C., M.R., W.C., S.M.S., M.L.G., M.K., and M.H. performed research; A.G.G., O.A.O., P.W.H., P.-Y.C.-H., A.P., K.S., M.H., Y.K., and M.M. analyzed data; and M.M. wrote the paper. This Direct Submission article had a prearranged editor. 1A.G.G. and O.A.O. contributed equally to this work. |
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| Snippet | Influenza remains a serious public health threat throughout the world. Vaccines and antivirals are available that can provide protection from infection.... |
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| SubjectTerms | Animals Antibodies Antibodies - genetics Antibodies - immunology Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antigens antiviral agents Antiviral drugs B-lymphocytes Biological Sciences Birds Cells Cross Reactions - genetics Cross Reactions - immunology Disease Outbreaks Disease resistance Epitopes Epitopes - genetics Epitopes - immunology genome Genomes Genomics H1N1 subtype influenza A virus Health risks Humans Immunological memory Infection Infections influenza Influenza A Influenza A virus Influenza A virus - genetics Influenza A virus - immunology Influenza A Virus, H1N1 Subtype - genetics Influenza A Virus, H1N1 Subtype - immunology Influenza A Virus, H5N1 Subtype - genetics Influenza A Virus, H5N1 Subtype - immunology Influenza in Birds - genetics Influenza in Birds - immunology Influenza Vaccines - genetics Influenza Vaccines - immunology Influenza, Human - genetics Influenza, Human - immunology Influenza, Human - prevention & control Lymphocytes B manufacturing Memory cells Mice Molecular Sequence Data Monoclonal antibodies Orthomyxoviridae pandemic Pandemics Proteins Public health swine Swine flu Vaccination Vaccines Viruses |
| Title | Human antibodies reveal a protective epitope that is highly conserved among human and nonhuman influenza A viruses |
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