Structure and function analysis of an antibody recognizing all influenza A subtypes
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Kallewaard, Nicole L.
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Corti, Davide
Humabs BioMed SA, Bellinzona, Switzerland
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Collins, Patrick J.
Mill Hill Laboratory, The Francis Crick Institute, London, UK
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Neu, Ursula
Mill Hill Laboratory, The Francis Crick Institute, London, UK
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McAuliffe, Josephine M.
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Benjamin, Ebony
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Wachter-Rosati, Leslie
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Palmer-Hill, Frances J.
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Yuan, Andy Q.
Department of Antibody Discovery and Protein Engineering, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Walker, Philip A.
Structural Biology Science Technology Platform, Mill Hill Laboratory, Francis Crick Institute, London, UK
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Vorlaender, Matthias K.
Mill Hill Laboratory, The Francis Crick Institute, London, UK
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Bianchi, Siro
Humabs BioMed SA, Bellinzona, Switzerland
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Guarino, Barbara
Humabs BioMed SA, Bellinzona, Switzerland
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De Marco, Anna
Humabs BioMed SA, Bellinzona, Switzerland
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Vanzetta, Fabrizia
Humabs BioMed SA, Bellinzona, Switzerland
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Agatic, Gloria
Humabs BioMed SA, Bellinzona, Switzerland
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Foglierini, Mathilde
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Pinna, Debora
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Fernandez-Rodriguez, Blanca
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Fruehwirth, Alexander
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Silacci, Chiara
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Ogrodowicz, Roksana W.
Structural Biology Science Technology Platform, Mill Hill Laboratory, Francis Crick Institute, London, UK
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Martin, Stephen R.
Structural Biology Science Technology Platform, Mill Hill Laboratory, Francis Crick Institute, London, UK
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Sallusto, Federica
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Suzich, JoAnn A.
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Lanzavecchia, Antonio
Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland - Institute for Microbiology, ETH Zurich, Switzerland
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Zhu, Qing
Department of Infectious Disease and Vaccines, MedImmune LLC, One MedImmune Way, Gaithersburg, USA
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Gamblin, Steven J.
Mill Hill Laboratory, The Francis Crick Institute, London, UK
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Skehel, John J.
Mill Hill Laboratory, The Francis Crick Institute, London, UK
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Published in:
- Cell. - 2016, vol. 166, no. 3, p. 596-608
English
Influenza virus remains a threat because of its ability to evade vaccine-induced immune responses due to antigenic drift. Here, we describe the isolation, evolution, and structure of a broad-spectrum human monoclonal antibody (mAb), MEDI8852, effectively reacting with all influenza A hemagglutinin (HA) subtypes. MEDI8852 uses the heavy-chain VH6-1 gene and has higher potency and breadth when compared to other anti-stem antibodies. MEDI8852 is effective in mice and ferrets with a therapeutic window superior to that of oseltamivir. Crystallographic analysis of Fab alone or in complex with H5 or H7 HA proteins reveals that MEDI8852 binds through a coordinated movement of CDRs to a highly conserved epitope encompassing a hydrophobic groove in the fusion domain and a large portion of the fusion peptide, distinguishing it from other structurally characterized cross- reactive antibodies. The unprecedented breadth and potency of neutralization by MEDI8852 support its development as immunotherapy for influenza virus-infected humans.
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Medicine
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https://n2t.net/ark:/12658/srd1319400
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