The glycosylation pattern of baculovirus expressed envelope protein E2 affects its ability to prevent infection with bovine viral diarrhoea virus.
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.
Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, UK.
A
A
Pande
B V
BV
Carr
S Y C
SY
Wong
K
K
Dalton
I M
IM
Jones
J W
JW
McCauley
B
B
Charleston
D000818:Animals; D016367:Baculoviridae / Q000235:genetics / Q000378:metabolism*; D002417:Cattle; D002478:Cells, Cultured; D001908:Diarrhea Viruses, Bovine Viral / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D006031:Glycosylation; D008297:Male; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*; D018411:Spodoptera / Q000821:virology; D013737:Testis / Q000166:cytology / Q000821:virology; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*
D011994:Recombinant Proteins; D014759:Viral Envelope Proteins; C076551:gp53, bovine viral diarrhea virus