Antigenic variants with amino acid deletions clarify a neutralizing epitope specific for influenza B virus Victoria group strains
- 1 September 2001
- journal article
- Published by Microbiology Society in Journal of General Virology
- Vol. 82 (9) , 2169-2172
- https://doi.org/10.1099/0022-1317-82-9-2169
Abstract
To study the neutralizing epitopes of influenza B virus Victoria group strains, two monoclonal antibodies (MAbs) were used to select antigenic variants of the virus. MAbs 10B8 and 8E6 were found to react with B/Victoria group strains in three tests, peroxidase–antiperoxidase staining, haemagglutination inhibition and neutralization tests; no reactivity with B/Yamagata group strains was observed. Analysis of the deduced amino acid sequences of 10B8-induced variants identified a single amino acid deletion at residue 165 or 170, as well as a single amino acid substitution at residues 164 (Asp→Tyr), 165 (Asn→Ser or Thr) or 203 (Lys→Thr or Asn). A single amino acid substitution at residue 241 (Pro→Ser) was observed in 8E6-induced variants. Three-dimensional analysis showed that the epitopes for both MAbs were situated in close proximity to each other. Since B/Yamagata group strains are characterized by amino acid deletions at residues 164–166, the epitope for MAb 10B8 is strictly specific for B/Victoria group strains.Keywords
This publication has 8 references indexed in Scilit:
- Rapid detection and identification of two lineages of influenza B strains with monoclonal antibodiesJournal of Virological Methods, 1999
- Evolutionary characteristics of influenza B virus since its first isolation in 1940: dynamic circulation of deletion and insertion mechanismArchiv für die gesamte Virusforschung, 1998
- Selection of neutralizing antibody escape mutants with type A influenza virus HA-specific polyclonal antisera: possible significance for antigenic driftEpidemiology and Infection, 1997
- Neutralization escape mutants of type A influenza virus are readily selected by antisera from mice immunized with whole virus: a possible mechanism for antigenic driftJournal of General Virology, 1994
- Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acidNature, 1988
- The antigenic structure of the influenza B virus hemagglutinin: Operational and topological mapping with monoclonal antibodiesVirology, 1985
- Evolution of influenza A and B viruses: conservation of structural features in the hemagglutinin genes.Proceedings of the National Academy of Sciences, 1982
- Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolutionNature, 1981