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

A. Pande, B. V. Carr, Simon Yuk Chun Wong, K. Dalton, I. M. Jones, J. W. Mccauley, B. Charleston

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19 Citations (Scopus)

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

Original languageEnglish
Pages (from-to)54-62
Number of pages8
JournalVirus Research
Volume114
DOIs
Publication statusPublished - 2005

Keywords

  • N-LINKED GLYCOSYLATION
  • HOG-CHOLERA VIRUS
  • E-RNS
  • INFLUENZA-VIRUS
  • FUSION ACTIVITY
  • DISEASE-VIRUS
  • GLYCOPROTEIN
  • HEMAGGLUTININ
  • GLYCANS
  • PESTIVIRUS

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