Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells. Brief report.
The fatty acid acylation of the cell-associated virus-specific proteins of mouse hepatitis virus (A 59-strain) was studied. 3H-palmitate label was associated with E2, one of the two virion glycoproteins and its intracellular precursor gp 150. A 110 K protein, the unglycosylated apoprotein of gp 150, accumulated by tunicamycin treatment, also incorporated radiolabeled palmitic acid. The addition of fatty acid to the MHV-A 59 E 2 protein is therefore not dependent on glycosylation.
D000215:Acylation; D005227:Fatty Acids / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D006517:Murine hepatitis virus / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology; D014764:Viral Proteins / Q000276:immunology / Q000378:metabolism*
D005227:Fatty Acids; D006023:Glycoproteins; D006898:Hydroxylamines; D014764:Viral Proteins; D014415:Tunicamycin; D019811:Hydroxylamine