Langat virus M protein is structurally homologous to prM

J Virol. 2001 Apr;75(8):3999-4001. doi: 10.1128/JVI.75.8.3999-4001.2001.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Viral / immunology
  • Antibody Specificity / immunology
  • Blotting, Western
  • Chlorocebus aethiops
  • Cross Reactions / immunology
  • Cytoplasm / virology
  • Encephalitis Viruses, Tick-Borne / chemistry
  • Encephalitis Viruses, Tick-Borne / immunology*
  • Flavivirus / immunology
  • Immune Sera / immunology
  • Molecular Sequence Data
  • Neutralization Tests
  • Sequence Alignment
  • Serology
  • Vero Cells
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / immunology*

Substances

  • Antibodies, Viral
  • Immune Sera
  • Viral Envelope Proteins
  • prM protein, Flavivirus