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

Authors :
Pande A
Carr BV
Wong SY
Dalton K
Jones IM
McCauley JW
Charleston B
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.

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