title: Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions.
abstract: 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.
authors.affiliation: Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
authors.forename: M A
authors.initials: MA
authors.lastname: Whitt
authors.forename: J K
authors.initials: JK
authors.lastname: Rose
mesh_terms: 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
chemical_list: C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D010169:Palmitic Acids; D014759:Viral Envelope Proteins; D019308:Palmitic Acid