Langat virus M protein is structurally homologous to prM

M. R. Holbrook, H. Wang, Alan Barrett

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 - 2001

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Langat virus
Tick-Borne Encephalitis Viruses
Flaviviridae
Flavivirus
virion
Virion
antiserum
Immune Sera
Proteins
proteins
tick-borne encephalitis
Tick-Borne Encephalitis
Protein Folding
Culicidae
Western blotting
protein synthesis
Western Blotting
Viruses
viruses

ASJC Scopus subject areas

  • Immunology

Cite this

Langat virus M protein is structurally homologous to prM. / Holbrook, M. R.; Wang, H.; Barrett, Alan.

In: Journal of Virology, Vol. 75, No. 8, 2001, p. 3999-4001.

Research output: Contribution to journalArticle

Holbrook, M. R. ; Wang, H. ; Barrett, Alan. / Langat virus M protein is structurally homologous to prM. In: Journal of Virology. 2001 ; Vol. 75, No. 8. pp. 3999-4001.
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