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Natural feline leukemia-virus variant escapes neutralization by a monoclonal-antibody via an amino-acid change outside the antibody-binding epitope

Academic Article
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Overview

authors

  • Nicolaisenstrouss, K.
  • Kumar, H. P. M.
  • Fitting, T.
  • Grant, C. K.
  • Elder, John

publication date

  • November 1987

journal

  • Journal of Virology  Journal

abstract

  • We have molecularly cloned a natural variant of feline leukemia virus subtype B. This isolate is unique in that it is not neutralized by a monoclonal antibody which neutralized all other feline leukemia virus isolates tested, including members of the A, B, and C subtypes. Western immunoblotting indicated that the monoclonal antibody was less able to bind to the gp70 of the resistant isolate (designated lambda B1) than to the gp70s of susceptible viruses. Nucleotide sequence analysis of the envelope gene of lambda B1 revealed a high degree of homology with the susceptible Snyder-Theilen, Gardner-Arnstein, and Rickard subtype B isolates, including the presence of a 5-amino-acid minimal binding epitope required for binding by the neutralizing monoclonal antibody. The only change within the vicinity of this epitope was in a single nucleotide, and this difference changed a proline residue to leucine three amino acids from the N terminus of the binding epitope. Competitive binding studies with synthetic peptides indicated that substitution of leucine for proline resulted in a 10-fold decrease in the ability of the peptide to compete for antibody binding to native antigen. The results are consistent with the interpretation that this amino acid change lowers the affinity of antibody binding, resulting in failure of the antibody to neutralize the variant virus.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Antigen-Antibody Complex
  • Antigens, Viral
  • Base Sequence
  • Cell Line
  • Epitopes
  • Genes
  • Genes, Viral
  • Genetic Variation
  • Leukemia Virus, Feline
  • Molecular Sequence Data
  • Neutralization Tests
  • Viral Envelope Proteins
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Identity

PubMed Central ID

  • PMC255936

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 2444714
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Additional Document Info

start page

  • 3410

end page

  • 3415

volume

  • 61

issue

  • 11

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