Abstract
Polypeptide analysis of three strains of human rotavirus (KUN, Wa and MO) were conducted using a hypertonic culture which suppressed host protein synthesis and unmasked rotavirus specific protein synthesis. As a result, eleven human rotavirus specific polypeptides (Vp 1--Vp 11) were detected by pulselabeling infected cells with [14C]-leucine. Among the 11 polypeptides, three polypeptides (Vp 7, Vp 10 and Vp 11) underwent post-translational processing, and two (Vp 7 and Vp 10) were glycosylated. Six polypeptides (Vp 1, 2, 3, 4, 6 and 7) were identified as viral structural proteins. Comparisons of three strains of different serotypes revealed that their polypeptide profiles differed from each other in electrophoretic mobility; in particular, profiles of the glycosylated polypeptide, Vp 7, were distinct among the three strains.
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