A revised nomenclature for the polypeptides of respiratory syncytial (RS) virus has been devised on the basis of comparison of the Long, A2 and RSN-2 strains by slab-gel electrophoresis. Seven polypeptides, now designated VP200, VGP48, VPN41, VPP32, VPM27, VP25 and VP10, were observed in preparations of all three strains of RS virus, irrespective of the host cell of origin. In addition, a slowly migrating glycopolypeptide GP1 was prominent in partially purified RS virus of the Long and A2 strains obtained from Hep-2 cells, and to a lesser extent from BS-C-1 cells. In the case of the RSN-2 strain, this polypeptide was only resolved clearly in virus obtained from Hep-2 cells. GP1 was an atypical glycopolypeptide in that S-methionine incorporation was poor relative to H-glucosamine incorporation.

The mutants of RS virus exhibited four distinct phenotypes with respect to intracellular polypeptide synthesis and antigen production at 39 °C. Mutants 17 (complementation group B′) and 19 (group E) were almost completely restricted, suggesting defective early functions. Mutants A1 (group A), A7 (group C) and 1 (group D) synthesized antigen and polypeptides normally, but the amount of antigen at the cell surface was reduced, suggesting maturation defects. In addition, the VPP32 of 1 (group D) exhibited an aberrant mobility, confirming its viral specificity. The remaining mutants, representing groups B, F and G exhibited generally impaired synthesis at 39 °C.

Absence of surface filaments in mutant-infected cells at 39 °C confirmed their virus-specific nature.


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