Structural difference in the fusion protein among strains of bovine respiratory syncytial virus.
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abstract
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.