1. Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein
- Author
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John R. Brubaker, Dennis W. Trent, Barbara J. B. Johnson, and John T. Roehrig
- Subjects
Hemagglutination ,viruses ,Molecular Sequence Data ,Alphavirus ,medicine.disease_cause ,Epitope ,Neutralization ,Virus ,Encephalitis Virus, Venezuelan Equine ,Epitopes ,Viral Envelope Proteins ,Viral envelope ,Neutralization Tests ,Sequence Homology, Nucleic Acid ,Virology ,medicine ,Animals ,Amino Acid Sequence ,Antigens, Viral ,Vero Cells ,Base Sequence ,Virulence ,biology ,Antibodies, Monoclonal ,Genetic Variation ,biology.organism_classification ,Mutation ,Venezuelan equine encephalitis virus ,Vero cell ,RNA, Viral ,Software - Abstract
Stable neutralization (N) escape variants of Venezuelan equine encephalitis (VEE) virus were selected by anti-E2 glycoprotein monoclonal antibodies (MAbs) that neutralize viral infectivity, block viral hemagglutination, and passively protect mice. The nucleotide sequence of the E1, E2, and E3 genes of four variants revealed a clustering of single mutations in a domain spanning E2-182 to E2-207. The conformation of this short linear sequence affects antigenicity in the N domain because reduction and alkylation of virus disrupted binding of some E2 neutralizing MAbs. Serologic evidence for interaction of E2 epitopes also was obtained. Mutations in the N domain of VEE virus did not alter the kinetics of binding to Vero cells. They did, in some cases, produce attenuation of virulence in mice.
- Published
- 1990
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