Infectious bronchitis virus (IBV), strain Beaudette, grown in cultured cells contained five structural proteins with apparent mol. wt. of 170000 (p170), 94000 (gp94), 50000 (pp50) 30000 (gp30) and 26000 (p26). Both gp94 and gp30 are glycopeptides since they were labelled with [H]glucosamine. The only phosphorylated polypeptide was pp50, and both it and gp94 were occasionally resolved into two bands. Two other polypeptides with mol. wt. of 28000 (p28) and 14000 (p14) were sometimes associated with the virus. In egg-grown virus two additional proteins were found with mol. wt. of 110000 (p110) and 75000 (gp75). The cell protein, actin, was also found in highly purified IBV virions. Different serotypes of either tissue culture-grown or egg-grown virus showed one of the two distinct polypeptide patterns of IBV described by Nagy & Lomniczi (1979) and Collins & Alexander (1980). Strain Beaudette gave a pattern characteristic of the M type, while strain Connecticut gave a pattern characteristic of the C type. The polypeptides present in Connecticut virus were p170, gp98, pp50, gp28 and p26. Thus, the differences between the two patterns involve the mobility of both the large (gp94/gp98) and small (gp30/gp28) glycopeptides.


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