Distinction of viral and host-derived glycopolypeptides induced by "early" functions of human cytomegalovirus.

Human cytomegalovirus is shown to induce in phosphonoacetic acid-treated human fibroblasts glycosylation of five polypeptides with approximate molecular weights of 200-250, 150, 135, 130 and 100 kilodaltons (kd). Except for the 130 kd product, these glycopolypeptides (gp) separate with the cytoplasmic fraction, only one (200-250 kd) with the chromatin fraction as well. The gp of 135 and 100 kd were found to be virus-specified as determined by immunoblotting and immunoprecipitation. The gp of 200-250 kd exhibited an immunological relatedness to fibronectin and are therefore considered host-specific products. Both subsets of gp participate in virus-induced surface membrane alterations as documented by living cell immunofluorescence.