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

Abstract

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.

• Authors: K Venugopal, S Y Shiu, E A Gould
• Journal: Research in veterinary science (Res Vet Sci) Vol. 57 Issue 2 Pg. 188-93 (Sep 1994) ISSN: 0034-5288 [Print] ENGLAND
• PMID: 7529419 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Antibodies, Monoclonal
• Antigens, Viral
• DNA Primers
• Epitopes
• Recombinant Proteins
• Viral Envelope Proteins

Topics

• 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)