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

Pande, A., Carr, B. V., Wong, S. Y. C., Dalton, K., Jones, I. M., McCauley, J. W. and Charleston, B. (2005) The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus. Virus Research, 114 (1-2). pp. 54-62. ISSN 0168-1702

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To link to this article DOI: 10.1016/j.virusres.2005.05.011

Abstract/Summary

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. (c) 2005 Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10371
Uncontrolled Keywords:N-LINKED GLYCOSYLATION, HOG-CHOLERA VIRUS, E-RNS, INFLUENZA-VIRUS, FUSION ACTIVITY, DISEASE-VIRUS, GLYCOPROTEIN, HEMAGGLUTININ, GLYCANS, PESTIVIRUS

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