Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions.
We have investigated the role of fatty acid acylation on two properties of the glycoprotein (G protein) from the Indiana serotype of vesicular stomatitis virus (VSV). Using a mutated G protein described previously (CS-2) that is not palmitylated, we found that fatty acid acylation was not required for the low pH-induced membrane fusion activity of VSV G protein. Transient expression of CS in HeLa cells resulted in syncytia formation that was indistinguishable from that induced by wild-type G protein. In addition, we found that expression of CS complemented a temperature-sensitive mutant of VSV (tsO45) as well as the wild-type protein. These results indicate that the presence of palmitate on the cytoplasmic domain of VSV G protein is not required for any step in the life cycle of the virus.
Whitt
M A
MA
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
Rose
J K
JK
D000215:Acylation; D005434:Flow Cytometry; D015870:Gene Expression / Q000502:physiology; D015726:Giant Cells / Q000382:microbiology; D006367:HeLa Cells; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008561:Membrane Fusion / Q000502:physiology*; D008562:Membrane Glycoproteins; D009154:Mutation / Q000235:genetics; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D013696:Temperature; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D014771:Virion / Q000378:metabolism
C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D010169:Palmitic Acids; D014759:Viral Envelope Proteins; D019308:Palmitic Acid