Respiratory syncytial virus proteins

Abstract

Respiratory syncytial (RS) virus grown in BS-C-1 cells was concentrated from the fluid of infected cultures by precipitation with polyethylene glycol (PEG) and banded by isopycnic centrifugation in sucrose or metrizamide density gradients. At least six virus-specified polypeptide bands, one of which was heterogeneous, could be resolved by continuous SDS-polyacrylamide gel electrophoresis (PAGE) and an additional band by discontinuous SDS-PAGE. The three predominant viral polypeptides were a glycopolypeptide of 48 × 10 3 (VGP48), a nucleocapsid polypeptide of 41 × 10 3 (VP41), and a polypeptide of 27 × 10 3 molecular weight (VP27). Three minor viral polypeptides have been assigned the molecular weight of 38 × 10 3 (VP38), 32 × 10 3 (VP32) and 25 × 10 3 (VP25). A minor glycopolypeptide of molecular weight 42 × 10 3 (VGP42) may exist also. Partial purification was accompanied by the loss of high molecular weight glycopolypeptides; however, one high molecular polypeptide (P2) remained consistently associated with the presumptive polypeptides and may represent an eighth virus-specified polypeptide. VP27 can be obtained in relatively pure form by sedimentation of detergent-treated RS virus in a metrizamide gradient containing detergent.