Recombinant vaccinia virus expressing PrM and E glycoproteins of louping ill virus: induction of partial homologous and heterologous protection in mice.

Recombinant vaccinia viruses expressing either the premembrane/truncated envelope (PrM/TrE) or truncated envelope (TrE) protein of louping ill virus were constructed. Both constructs expressed authentic E proteins as determined by their size and antigenic reactivity with a panel of monoclonal antibodies. The deletion of the C-terminal hydrophobic domain of the envelope glycoprotein resulted in the secretion of E protein into the supernatant culture medium. The immunisation of mice with these recombinant viruses showed that the recombinant expressing PrM/TrE proteins induced neutralising and protective antibodies against challenge with louping ill or tick-borne encephalitis virus, but that the recombinant expressing the E or the TrE protein alone failed to induce any detectable immune responses against homologous or heterologous virus challenge.
AuthorsK Venugopal, S Y Shiu, E A Gould
JournalResearch in veterinary science (Res Vet Sci) Vol. 57 Issue 2 Pg. 188-93 (Sep 1994) ISSN: 0034-5288 [Print] ENGLAND
PMID7529419 (Publication Type: Comparative Study, Journal Article)
Chemical References
  • Antibodies, Monoclonal
  • Antigens, Viral
  • DNA Primers
  • Epitopes
  • Recombinant Proteins
  • Viral Envelope Proteins
  • Animals
  • Antibodies, Monoclonal
  • Antigens, Viral (biosynthesis, immunology)
  • Base Sequence
  • Cell Line
  • DNA Primers
  • Encephalitis Viruses, Tick-Borne (genetics, immunology)
  • Epitopes (analysis)
  • Fluorescent Antibody Technique
  • Kidney
  • Mice
  • Molecular Sequence Data
  • Recombinant Proteins (biosynthesis, immunology)
  • Recombination, Genetic
  • Sequence Deletion
  • Swine
  • Transfection
  • Vaccinia virus (genetics, immunology)
  • Viral Envelope Proteins (biosynthesis, immunology)

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