The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus.
Virus Res
; 114(1-2): 54-62, 2005 Dec.
Article
em En
| MEDLINE
| ID: mdl-15993973
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes
/
Proteínas do Envelope Viral
/
Baculoviridae
/
Vírus da Diarreia Viral Bovina
Limite:
Animals
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article