Structural difference in the fusion protein among strains of bovine respiratory syncytial virus.
The polypeptides of different strains of bovine respiratory syncytial virus (RSV) were compared. Altered electrophoretic migrations were observed in the G, F, P, M and 22 kDa polypeptides. The molecular weight of the F2 fragment in human RSV (Long strain) and bovine RSV (A51908 and Md-X strains) was approximately 20 kDa whereas it was approximately 15.5 kDa in caprine RSV and bovine RSV (FS-1 and VC-464 strains). The size difference of the F2 subunit was due to difference in the extent of glycosylation.
Mallipeddi
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Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park.
Samal
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D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D008970:Molecular Weight; D011233:Precipitin Tests; D018112:Respiratory Syncytial Virus, Bovine / Q000737:chemistry*; D014760:Viral Fusion Proteins / Q000737:chemistry*
D014760:Viral Fusion Proteins