Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein

Barbara J B Johnson, John R. Brubaker, John T. Roehrig, Dennis W. Trent

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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 Et, 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.

Original languageEnglish
Pages (from-to)676-683
Number of pages8
JournalVirology
Volume177
Issue number2
DOIs
StatePublished - 1990

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Venezuelan Equine Encephalitis Viruses
Viral Hemagglutination
Glycoproteins
Monoclonal Antibodies
Virus Attachment
Mutation
Vero Cells
Alkylation
Neutralizing Antibodies
Cluster Analysis
Virulence
Epitopes
Genes

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

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Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein. / Johnson, Barbara J B; Brubaker, John R.; Roehrig, John T.; Trent, Dennis W.

In: Virology, Vol. 177, No. 2, 1990, p. 676-683.

Research output: Contribution to journalArticle

Johnson, Barbara J B ; Brubaker, John R. ; Roehrig, John T. ; Trent, Dennis W. / Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein. In: Virology. 1990 ; Vol. 177, No. 2. pp. 676-683.
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