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A common solution to group 2 influenza virus neutralization

Academic Article
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Overview

related to degree

  • Lee, Peter S., Ph.D. in Biology, Scripps Research 2009 - 2014
  • Bhabha, Gira Sorab, Ph.D. in Biology, Scripps Research 2006 - 2011
  • Ekiert, Damian, Ph.D. in Chemical Biology, Scripps Research 2006 - 2011

authors

  • Friesen, R. H. E.
  • Lee, Peter S.
  • Stoop, E. J. M.
  • Hoffman, R. M. B.
  • Ekiert, Damian
  • Bhabha, Gira Sorab
  • Yu, W.
  • Juraszek, J.
  • Koudstaal, W.
  • Jongeneelen, M.
  • Korse, H. J. W. M.
  • Ophorst, C.
  • Brinkman-van der Linden, E. C. M.
  • Throsby, M.
  • Kwakkenbos, M. J.
  • Bakker, A. Q.
  • Beaumont, T.
  • Spits, H.
  • Kwaks, T.
  • Vogels, R.
  • Ward, Andrew
  • Goudsmit, J.
  • Wilson, Ian

publication date

  • January 2014

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The discovery and characterization of broadly neutralizing antibodies (bnAbs) against influenza viruses have raised hopes for the development of monoclonal antibody (mAb)-based immunotherapy and the design of universal influenza vaccines. Only one human bnAb (CR8020) specifically recognizing group 2 influenza A viruses has been previously characterized that binds to a highly conserved epitope at the base of the hemagglutinin (HA) stem and has neutralizing activity against H3, H7, and H10 viruses. Here, we report a second group 2 bnAb, CR8043, which was derived from a different germ-line gene encoding a highly divergent amino acid sequence. CR8043 has in vitro neutralizing activity against H3 and H10 viruses and protects mice against challenge with a lethal dose of H3N2 and H7N7 viruses. The crystal structure and EM reconstructions of the CR8043-H3 HA complex revealed that CR8043 binds to a site similar to the CR8020 epitope but uses an alternative angle of approach and a distinct set of interactions. The identification of another antibody against the group 2 stem epitope suggests that this conserved site of vulnerability has great potential for design of therapeutics and vaccines.

subject areas

  • Animals
  • Antibodies
  • Antibodies, Monoclonal
  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Chromatography, Gel
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Female
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Humans
  • Immunologic Memory
  • Influenza A virus
  • Influenza Vaccines
  • Kinetics
  • Mice
  • Mice, Inbred BALB C
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Conformation
  • Species Specificity
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Research

keywords

  • X-ray crystallography
  • antibody recognition
  • electron microscopy
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Identity

PubMed Central ID

  • PMC3890827

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.1319058110

PubMed ID

  • 24335589
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Additional Document Info

start page

  • 445

end page

  • 450

volume

  • 111

issue

  • 1

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