Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus
Identifieur interne : 001F70 ( Main/Curation ); précédent : 001F69; suivant : 001F71Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus
Auteurs : A. I. Klimov [Russie] ; S. G. Markushin [Russie] ; S. Prösch [Allemagne] ; V. P. Ginzburg [Russie] ; H. Heider [Allemagne] ; A. M. Heider [Russie] ; C. Schröeder [Allemagne] ; R. G. Webster [États-Unis]Source :
- Archives of Virology [ 0304-8608 ] ; 1992-03-01.
English descriptors
- Teeft :
- Amantadine, Amino, Amino acid substitutions, Antigenic, Antigenic sites, Antigenic specificities, Antigenic specificity, Arch virol, Different positions, Drug resistance, Fowl, Fowl plague virus, Haemagglutinating, Haemagglutinating activity, Haemagglutinin, Heider, Influenza, Influenza virus, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutant, Mutation, Norakin, Rimantadine, Substitution, Virol, Virus, Virus strains.
Abstract
Summary: Norakin-resistant (NR) mutants of fowl plague virus (A/FPV/Wey-bridge, H7N7) have 1 to 2 (in one instance 3) amino acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. This potential effect should be taken into account when antiviral substances directed to surface influenza virus antigens are being developed for use as antiviral drugs.
Url:
DOI: 10.1007/BF01314632
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<term>Antigenic sites</term>
<term>Antigenic specificities</term>
<term>Antigenic specificity</term>
<term>Arch virol</term>
<term>Different positions</term>
<term>Drug resistance</term>
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<term>Fowl plague virus</term>
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<term>Haemagglutinating activity</term>
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<term>Influenza virus</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
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<term>Mutant</term>
<term>Mutation</term>
<term>Norakin</term>
<term>Rimantadine</term>
<term>Substitution</term>
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<front><div type="abstract" xml:lang="en">Summary: Norakin-resistant (NR) mutants of fowl plague virus (A/FPV/Wey-bridge, H7N7) have 1 to 2 (in one instance 3) amino acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. This potential effect should be taken into account when antiviral substances directed to surface influenza virus antigens are being developed for use as antiviral drugs.</div>
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