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The receptor-binding and membrane-fusion properties of influenza-virus variants selected using anti-hemagglutinin monoclonal-antibodies

Academic Article
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Overview

authors

  • Daniels, R. S.
  • Jeffries, S.
  • Yates, P.
  • Schild, G. C.
  • Rogers, G. N.
  • Paulson, James
  • Wharton, S. A.
  • Douglas, A. R.
  • Skehel, J. J.
  • Wiley, D. C.

publication date

  • May 1987

journal

  • EMBO Journal  Journal

abstract

  • A monoclonal antibody raised against X-31 influenza virus reacted with the majority of natural H3N2 viruses isolated between 1968 and 1982. A number of variants of X-31 and of a receptor-binding mutant of X-31 were selected by the antibody during virus replication in eggs and MDCK cells. Antibody-binding assays indicated that the viruses selected were not antigenic variants and analyses using derivatized erythrocytes showed that their receptor-binding properties differed from those of the parent viruses. The amino acid substitutions in the variants were all located in the vicinity of the receptor-binding site and the structural consequences are discussed in relation to the three-dimensional structure of X-31 HA. In addition all of the variants fused membranes at higher pH than wild-type virus indicating that structural modifications in the distal globular region of HA influence the low pH-induced conformational change required for membrane fusion.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Genetic Variation
  • Hemagglutination Inhibition Tests
  • Hemagglutinins, Viral
  • Influenza A virus
  • Mice
  • Mice, Inbred BALB C
  • Mutation
  • Receptors, Virus
  • Species Specificity
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Identity

PubMed Central ID

  • PMC553952

International Standard Serial Number (ISSN)

  • 0261-4189

PubMed ID

  • 3608984
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Additional Document Info

start page

  • 1459

end page

  • 1465

volume

  • 6

issue

  • 5

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