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Phosphoprotein profile analysis of ruminant respiratory syncytial virus isolates
S V Shadomy1, J C Baker, M A Mufson
1Department of Large Animal Clinical Sciences, Michigan State University, East Lansing 48824, USA.
Objective:
To determine the apparent molecular weight for 24 ruminant respiratory syncytial viruses (RSV) on the basis of differences in the electrophoretic mobility of the phosphoprotein (P protein).
Procedure:
29 bovine RSV (BRSV), 20 of which were not previously tested, 3 ovine RSV, and 1 caprine RSV isolates were selected for determination of electrophoretic mobility of the P protein. Virus radiolabeled with [35S]methionine was immunoprecipitated with polyclonal antiserum to BRSV and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Results:
On the basis of apparent molecular size of the P protein, all isolates could be categorized into 2 electropherotypes, low molecular size of 36 kd and high molecular size of 38 kd. Twenty-three BRSV, the 3 ovine RSV, and 1 caprine RSV isolates had a high molecular size P protein; 6 BRSV isolates had a low molecular size P protein.
Conclusions:
The apparent molecular size of the P protein of the ruminant RSV strains is greater than that of the human RSV subgroups, providing further evidence of their distinctiveness. Whether categorization of electrophoretic mobility of the P protein of BRSV underlies distinct antigenic subgroups, as it does in human RSV, requires further antigenic and genetic analysis.
Clinical Relevance:
Antigenic subgroups of ruminant RSV may have relevance in the development of new vaccines for control of the disease.