Multiple amino acid substitutions in the HN protein of the paramyxovirus, SV5, are selected for in monoclonal antibody resistant mutants

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Abstract

Monoclonal antibody resistant (MAR) mutants (which escaped antibody-mediated neutralization) were selected from simian (W 3) and human (LN) isolates of simian virus 5 (SV 5), using monoclonal antibodies (MAbs) specific for antigenic sites 4 and 5 on the HN glycoprotein. Resistance correlated with an inability of the selecting antibody to bind with the respective MAR mutants. Sequence comparisons between parental and mutant HN proteins revealed multiple non-adjacent amino acid substitutions in the majority of MAR mutants. The same multiple substitutions were identified in mutants selected from both the LN and W 3 isolates of SV 5. Furthermore, different mutations on the primary sequence of the HN protein conferred resistance to the same MAb.

Original languageEnglish
Pages (from-to)217-24
Number of pages8
JournalArchives of Virology
Volume131
Issue number02-Jan
Publication statusPublished - 1993

Keywords

  • HEMAGGLUTININ NEURAMINIDASE GLYCOPROTEIN
  • PARAINFLUENZA VIRUS TYPE-2
  • SEQUENCE-ANALYSIS
  • SIMIAN VIRUS-5
  • NUCLEOTIDE-SEQUENCE
  • MESSENGER-RNA
  • SENDAI VIRUS
  • PATHOGENICITY

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