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Structure of the apo anti-influenza CH65 Fab

Academic Article
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Overview

related to degree

  • Lee, Peter S., Ph.D. in Biology, Scripps Research 2009 - 2014

authors

  • Lee, Peter S.
  • Arnell, A. J.
  • Wilson, Ian

publication date

  • February 2015

journal

  • Acta Crystallographica Section F-Structural Biology Communications  Journal

abstract

  • Influenza viruses remain a persistent challenge to human health owing to their inherent ability to evade the immune response by antigenic drift. However, the discovery of broadly neutralizing antibodies (bnAbs) against divergent viruses has sparked renewed interest in a universal influenza vaccine and novel therapeutic opportunities. Here, a crystal structure at 1.70 Å resolution is presented of the Fab of the human antibody CH65, which has broad neutralizing activity against a range of seasonal H1 isolates. Previous studies proposed that affinity maturation of this antibody lineage pre-organizes the complementarity-determining region (CDR) loops into an energetically favorable HA-bound conformation. Indeed, from the structural comparisons of free and HA-bound CH65 presented here, the CDR loops, and in particular the heavy-chain CDR3, adopt the same conformations in the free and bound forms. Thus, these findings support the notion that affinity maturation of the CH65 lineage favorably preconfigures the CDR loops for high-affinity binding to influenza hemagglutinin.

subject areas

  • Antibodies, Neutralizing
  • Apoproteins
  • Crystallography, X-Ray
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Humans
  • Immunoglobulin Fab Fragments
  • Influenza A virus
  • Models, Molecular
  • Protein Binding
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Research

keywords

  • adaptive immunity
  • affinity maturation
  • antibody
  • influenza
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Identity

PubMed Central ID

  • PMC4321466

International Standard Serial Number (ISSN)

  • 1744-3091

Digital Object Identifier (DOI)

  • 10.1107/s2053230x14027599

PubMed ID

  • 25664786
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Additional Document Info

start page

  • 145

end page

  • 148

volume

  • 71

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