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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Baculoviridae / genetics
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Baculoviridae / metabolism*
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Cattle
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Cells, Cultured
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Diarrhea Viruses, Bovine Viral / genetics
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Diarrhea Viruses, Bovine Viral / metabolism
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Diarrhea Viruses, Bovine Viral / pathogenicity*
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Glycosylation
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Male
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Mutagenesis, Site-Directed
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism*
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Spodoptera / virology
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Testis / cytology
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Testis / virology
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Viral Envelope Proteins / genetics
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Viral Envelope Proteins / metabolism*
Substances
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Recombinant Proteins
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Viral Envelope Proteins
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gp53, bovine viral diarrhea virus