Langat virus M protein is structurally homologous to prM

M. R. Holbrook, H. Wang, A. D.T. Barrett

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

Langat (LGT) virus M protein has been generated in a recombinant system. Antiserum raised against the LGT virus M protein neutralizes tick-borne encephalitis serocomplex flaviviruses but not mosquito-borne flaviviruses, indicating that the M protein is exposed on the surface of virions. The antiserum recognizes intracellular LGT virus prM/M and binds to prM and M in Western blots of whole-cell lysates and purified virus, respectively. These data suggest that the prM and M proteins are structurally similar under native conditions and support the hypothesis that the "pr" portion of prM facilitates proper folding of the M protein for expression on the virion surface.

Original languageEnglish (US)
Pages (from-to)3999-4001
Number of pages3
JournalJournal of virology
Volume75
Issue number8
DOIs
StatePublished - Apr 10 2001

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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