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.
Baty
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DU
School of Biological and Medical Sciences, University of St. Andrews, Scotland.
Randall
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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