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.
Radsak
K
K
Mertensmaier
I
I
Kaiser
C
C
Wagner
C
C
D000954:Antigens, Surface / Q000096:biosynthesis; D000956:Antigens, Viral / Q000096:biosynthesis; D050260:Carbohydrate Metabolism; D002478:Cells, Cultured; D003587:Cytomegalovirus / Q000502:physiology*; D005347:Fibroblasts / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis*; D006801:Humans; D007158:Immunologic Techniques; D008297:Male; D008970:Molecular Weight; D010413:Penis; D010455:Peptides / Q000302:isolation & purification*; D011499:Protein Processing, Post-Translational; D014764:Viral Proteins / Q000096:biosynthesis*
D000954:Antigens, Surface; D000956:Antigens, Viral; D005353:Fibronectins; D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins