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The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus.
- Source :
-
Virus research [Virus Res] 2005 Dec; Vol. 114 (1-2), pp. 54-62. Date of Electronic Publication: 2005 Jul 01. - Publication Year :
- 2005
-
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.
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 0168-1702
- Volume :
- 114
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Virus research
- Publication Type :
- Academic Journal
- Accession number :
- 15993973
- Full Text :
- https://doi.org/10.1016/j.virusres.2005.05.011