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Journal of Virology, January 1999, p. 787-790, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of a Natural Mutation in an Antigenic Site on the Fusion Protein of Measles Virus That Is Involved in Neutralization

Joël Fayolle,1 Bernard Verrier,2 Robin Buckland,1 and T. Fabian Wild1,*

Unité INSERM 404 "Immunity and Vaccination," Bâtiment Ex-Institut Pasteur de Lyon, 69372 Lyon Cedex 07,1 and UMR 103 CNRS-BIOMERIEUX, Ecole Normale Supérieure de Lyon, 69364 Lyon Cedex 07,2 France

Received 27 July 1998/Accepted 8 October 1998

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 (Rright-arrowW) was observed. The possibility of selecting measles virus variants in vaccinated populations is discussed.

* Corresponding author. Mailing address: Unité INSERM 404, Immunité et Vaccination, Bâtiment Ex-Institut Pasteur de Lyon, Avenue Tony Garnier, 69372 Lyon Cedex 07, France. Phone: 33 4 72 72 25 53. Fax: 33 4 72 72 25 67. E-mail: wild{at}lyon151.inserm.fr.

Journal of Virology, January 1999, p. 787-790, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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