A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface.
We investigated the role of glycosylation in intracellular transport and cell surface expression of the vesicular stomatitis virus glycoprotein (G) in cells expressing G protein from cloned cDNA. The individual contributions of the two asparagine-linked glycans of G protein to cell surface expression were assessed by site-directed mutagenesis of the coding sequence to eliminate one or the other or both of the glycosylation sites. One oligosaccharide at either position was sufficient for cell surface expression of G protein in transfected cells, and the rates of oligosaccharide processing were similar to the rate observed for wild-type protein. However, the nonglycosylated G protein synthesized when both glycosylation sites were eliminated did not reach the cell surface. This protein did appear to reach a Golgi-like region, as determined by indirect immunofluorescence microscopy, however, and was modified with palmitic acid. It was also apparently not subject to increased proteolytic breakdown.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D007668:Kidney; D008562:Membrane Glycoproteins; D009154:Mutation; D009844:Oligosaccharides / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics* / Q000378:metabolism; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism
C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D004247:DNA