title: Characterization of a natural mutation in an antigenic site on the fusion protein of measles virus that is involved in neutralization.
abstract: Although measles virus is an antigenically monotypic virus, nucleotide sequence analysis of the hemagglutinin and nucleoprotein genes has permitted the differentiation of a number of genotypes. In contrast, the fusion (F) protein is highly conserved; only three amino acid changes have been reported over a 40-year period. We have isolated a measles virus strain which did not react with an anti-F monoclonal antibody (MAb) which we had previously shown to be directed against a dominant antigenic site. This virus strain, Lys-1, had seven amino acid changes compared with the Edmonston strain. We have shown that a single amino acid at position 73 is responsible for its nonreactivity with the anti-F MAb. With the same MAb, antibody-resistant mutants were prepared from the vaccine strain. A single amino acid change at position 73 (R-->W) was observed. The possibility of selecting measles virus variants in vaccinated populations is discussed.
authors.affiliation: Unité INSERM 404 "Immunity and Vaccination," Bâtiment Ex-Institut Pasteur de Lyon, 69372 Lyon Cedex 07, France.
authors.forename: J
authors.initials: J
authors.lastname: Fayolle
authors.forename: B
authors.initials: B
authors.lastname: Verrier
authors.forename: R
authors.initials: R
authors.lastname: Buckland
authors.forename: T F
authors.initials: TF
authors.lastname: Wild
mesh_terms: D000911:Antibodies, Monoclonal / Q000276:immunology*; D000956:Antigens, Viral / Q000276:immunology*; D006801:Humans; D008458:Measles Vaccine / Q000276:immunology; D008459:Measles virus / Q000235:genetics / Q000276:immunology*; D009154:Mutation; D013329:Structure-Activity Relationship; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000276:immunology*
chemical_list: D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D008458:Measles Vaccine; D014760:Viral Fusion Proteins