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1. The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus.

Author

Pande A, Carr BV, Wong SY, Dalton K, Jones IM, McCauley JW, and Charleston B

Subjects
Animals, Baculoviridae genetics, Cattle, Cells, Cultured, Diarrhea Viruses, Bovine Viral genetics, Diarrhea Viruses, Bovine Viral metabolism, Glycosylation, Male, Mutagenesis, Site-Directed, Recombinant Proteins genetics, Spodoptera virology, Testis cytology, Testis virology, Viral Envelope Proteins genetics, Baculoviridae metabolism, Diarrhea Viruses, Bovine Viral pathogenicity, Recombinant Proteins metabolism, Viral Envelope Proteins metabolism
Abstract

We have investigated the role of glycosylation of the envelope glycoprotein E2 of bovine viral diarrhoea virus (BVDV), produced in insect cells, in BVDV infection. When amino acids predicated to code for the C-terminal N-linked glycosylation site were mutated the resulting protein was less efficient than wild type protein at preventing infection of susceptible cells with BVDV. In addition, mutational analysis showed that a further two predicted N-terminal N-linked glycosylation sites of E2 are required for efficient production of recombinant protein.

Published
2005
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