Multiple amino acid substitutions in the HN protein of the paramyxovirus, SV5, are selected for in monoclonal antibody resistant mutants.
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.
School of Biological and Medical Sciences, University of St. Andrews, Scotland.
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Baty
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Randall
D000596:Amino Acids / Q000737:chemistry / Q000235:genetics; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D015707:HN Protein / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D006801:Humans; D009154:Mutation; D009500:Neutralization Tests; D018108:Respirovirus / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D014709:Vero Cells
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D015707:HN Protein