Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism
Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of i...
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| Published in | Cell Vol. 177; no. 5; pp. 1124 - 1135.e16 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
16.05.2019
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular “breathing” of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in “universal” flu vaccines.
[Display omitted]
•Human B cells specific for a novel epitope on influenza A groups 1 and 2•Crystallography locates the epitope at the interface of the hemagglutinin head domains•Robust protection by antibodies to this epitope, dependent on IgG subclass•Protective, cross-group antibodies are encoded by diverse sets of Ig gene segments
Antibodies targeting a novel site at the interface of the head domains of hemagglutinin provide broad, IgG-subclass-dependent protection against influenza. |
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| AbstractList | Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection
in vitro
, but passive administration to mice affords robust, IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular “breathing” of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in “universal” flu vaccines.
Antibodies targeting a novel site at the interface of the head domains of hemagglutinin provide broad protection against influenza that is IgG subclass dependent. Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular “breathing” of the HA trimer can expose the interface to antibody and B cells. Lastly, antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in “universal” flu vaccines. Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular "breathing" of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in "universal" flu vaccines. Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular “breathing” of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in “universal” flu vaccines. [Display omitted] •Human B cells specific for a novel epitope on influenza A groups 1 and 2•Crystallography locates the epitope at the interface of the hemagglutinin head domains•Robust protection by antibodies to this epitope, dependent on IgG subclass•Protective, cross-group antibodies are encoded by diverse sets of Ig gene segments Antibodies targeting a novel site at the interface of the head domains of hemagglutinin provide broad, IgG-subclass-dependent protection against influenza. Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular “breathing” of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in “universal” flu vaccines. Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular "breathing" of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in "universal" flu vaccines.Vaccines to generate durable humoral immunity against antigenically evolving pathogens such as the influenza virus must elicit antibodies that recognize conserved epitopes. Analysis of single memory B cells from immunized human donors has led us to characterize a previously unrecognized epitope of influenza hemagglutinin (HA) that is immunogenic in humans and conserved among influenza subtypes. Structures show that an unrelated antibody from a participant in an experimental infection protocol recognized the epitope as well. IgGs specific for this antigenic determinant do not block viral infection in vitro, but passive administration to mice affords robust IgG subtype-dependent protection against influenza infection. The epitope, occluded in the pre-fusion form of HA, is at the contact surface between HA head domains; reversible molecular "breathing" of the HA trimer can expose the interface to antibody and B cells. Antigens that present this broadly immunogenic HA epitope may be good candidates for inclusion in "universal" flu vaccines. |
| Author | Onodera, Taishi Caradonna, Timothy M. Adachi, Yu Song, Shengli Kelsoe, Garnett Kepler, Thomas B. Kuraoka, Masayuki McCarthy, Kevin R. Schmidt, Aaron G. Tonouchi, Keisuke Bajic, Goran McGee, Charles E. Takahashi, Yoshimasa Sempowski, Gregory D. Feng, Feng Harrison, Stephen C. Watanabe, Akiko Urick, Patricia |
| AuthorAffiliation | 9 Contributed equally 2 Departments of Pathology, Duke University, Durham, NC 27710, USA 5 Ragon Institute and Harvard Medical School, Cambridge, MA 02139, USA 4 Laboratory of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA 3 Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA 8 USA Howard Hughes Medical Institute, Boston, MA 02115, USA 1 Departments of Immunology, Duke University, Durham, NC 27710, USA 6 Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan 7 Department of Microbiology, Boston University School of Medicine, Boston, MA 02118 |
| AuthorAffiliation_xml | – name: 9 Contributed equally – name: 2 Departments of Pathology, Duke University, Durham, NC 27710, USA – name: 7 Department of Microbiology, Boston University School of Medicine, Boston, MA 02118 – name: 3 Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – name: 8 USA Howard Hughes Medical Institute, Boston, MA 02115, USA – name: 1 Departments of Immunology, Duke University, Durham, NC 27710, USA – name: 5 Ragon Institute and Harvard Medical School, Cambridge, MA 02139, USA – name: 4 Laboratory of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA – name: 6 Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan |
| Author_xml | – sequence: 1 givenname: Akiko surname: Watanabe fullname: Watanabe, Akiko organization: Department of Immunology, Duke University, Durham, NC 27710, USA – sequence: 2 givenname: Kevin R. surname: McCarthy fullname: McCarthy, Kevin R. organization: Laboratory of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA – sequence: 3 givenname: Masayuki surname: Kuraoka fullname: Kuraoka, Masayuki organization: Department of Immunology, Duke University, Durham, NC 27710, USA – sequence: 4 givenname: Aaron G. surname: Schmidt fullname: Schmidt, Aaron G. organization: Ragon Institute and Harvard Medical School, Cambridge, MA 02139, USA – sequence: 5 givenname: Yu surname: Adachi fullname: Adachi, Yu organization: Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 6 givenname: Taishi surname: Onodera fullname: Onodera, Taishi organization: Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 7 givenname: Keisuke surname: Tonouchi fullname: Tonouchi, Keisuke organization: Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 8 givenname: Timothy M. surname: Caradonna fullname: Caradonna, Timothy M. organization: Ragon Institute and Harvard Medical School, Cambridge, MA 02139, USA – sequence: 9 givenname: Goran surname: Bajic fullname: Bajic, Goran organization: Laboratory of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA – sequence: 10 givenname: Shengli surname: Song fullname: Song, Shengli organization: Department of Immunology, Duke University, Durham, NC 27710, USA – sequence: 11 givenname: Charles E. surname: McGee fullname: McGee, Charles E. organization: Duke Human Vaccine Institute, Duke University, Durham, NC 27710, USA – sequence: 12 givenname: Gregory D. surname: Sempowski fullname: Sempowski, Gregory D. organization: Department of Pathology, Duke University, Durham, NC 27710, USA – sequence: 13 givenname: Feng surname: Feng fullname: Feng, Feng organization: Department of Microbiology, Boston University School of Medicine, Boston, MA 02118, USA – sequence: 14 givenname: Patricia surname: Urick fullname: Urick, Patricia organization: Department of Microbiology, Boston University School of Medicine, Boston, MA 02118, USA – sequence: 15 givenname: Thomas B. surname: Kepler fullname: Kepler, Thomas B. organization: Department of Microbiology, Boston University School of Medicine, Boston, MA 02118, USA – sequence: 16 givenname: Yoshimasa surname: Takahashi fullname: Takahashi, Yoshimasa organization: Department of Immunology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan – sequence: 17 givenname: Stephen C. surname: Harrison fullname: Harrison, Stephen C. email: harrison@crystal.harvard.edu organization: Laboratory of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115, USA – sequence: 18 givenname: Garnett orcidid: 0000-0002-8770-040X surname: Kelsoe fullname: Kelsoe, Garnett email: ghkelsoe@duke.edu organization: Department of Immunology, Duke University, Durham, NC 27710, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31100267$$D View this record in MEDLINE/PubMed https://www.osti.gov/servlets/purl/1524669$$D View this record in Osti.gov |
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| Copyright | 2019 Elsevier Inc. Copyright © 2019 Elsevier Inc. All rights reserved. |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 National Institutes of Health (NIH). National Institute of General Medical Sciences (NIGMS) USDOE Office of Science (SC) AC02-06CH11357; P41 GM103403; JP18fk0108051; P01 AI089618; U19 AI117892; R01 AI128832 AUTHOR CONTRIBUTIONS: G.K., M.K., Y.T., and S.C.H. designed research; A.W., K.R.M., M.K., A.G.S. Y.A., T.O., K.T., and T.M.C. performed research; F.F., P.U., and T.B.K. recruited and managed human subject materials; S.S., G.B, C.E.M., and G.D.S. provided critical reagents and assays; A.W., K.R.M., M.K., A.G.S., T.B.K., T.M.C., Y.T, S.C.H., and G.K. analyzed data; A.W. K.R.M., M.K., Y.T., S.C.H., and G.K. wrote the paper. T.M.C., G.B., T.B.K., and C.E.M. edited and revised the paper. |
| ORCID | 0000-0002-8770-040X 000000028770040X |
| OpenAccessLink | https://www.osti.gov/servlets/purl/1524669 |
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| SubjectTerms | Adult Animals antibodies Antibodies, Viral - immunology B-lymphocytes BASIC BIOLOGICAL SCIENCES Dogs epitopes Epitopes - immunology Female Hemagglutinin Glycoproteins, Influenza Virus - immunology hemagglutinins Humans humoral immunity immunoglobulin G Immunoglobulin G - immunology influenza Influenza A virus - immunology influenza vaccines Influenza Vaccines - immunology Madin Darby Canine Kidney Cells Male Mice Middle Aged Orthomyxoviridae Orthomyxoviridae Infections - immunology Orthomyxoviridae Infections - pathology Orthomyxoviridae Infections - prevention & control pathogens |
| Title | Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism |
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