Respiratory syncytial virus proteins |
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Authors: | W.H. Wunner C.R. Pringle |
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Affiliation: | M. R. C. Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, Scotland |
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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 × 103 (VGP48), a nucleocapsid polypeptide of 41 × 103 (VP41), and a polypeptide of 27 × 103 molecular weight (VP27). Three minor viral polypeptides have been assigned the molecular weight of 38 × 103 (VP38), 32 × 103 (VP32) and 25 × 103 (VP25). A minor glycopolypeptide of molecular weight 42 × 103 (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. |
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Keywords: | Author to whom reprint request should be addressed. |
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