Assembly of viral membranes: maturation of the vesicular stomatitis virus glycoprotein in the presence of tunicamycin.
The role of glycosylation in the maturation of the vesicular stomatitis virus (VSV) glycoprotein was studied by use of the antibiotic tunicamycin. Tunicamycin-treated VSV-infected cells synthesize an unglycosylated form of the VSV glycoprotein (R. Leavitt, S. Schlesinger, and S. Kornfeld, J. Virol. 21:375--385, 1977). We have found that tunicamycin has no effect on the attachment of the glycoprotein to intracellular membranes or on the transport of protein to the lumen of the endoplasmic reticulum. However, tunicamycin prevented the migration of the glycoprotein from the rough endoplasmic reticulum to smooth intracellular membranes.
D002460:Cell Line; D005944:Glucosamine / Q000031:analogs & derivatives*; D006023:Glycoproteins / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D013347:Subcellular Fractions; D014415:Tunicamycin / Q000494:pharmacology*; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects* / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
D006023:Glycoproteins; D014764:Viral Proteins; D014415:Tunicamycin; D005944:Glucosamine