Myristylation of the envelope glycoprotein of vesicular stomatitis virus.
The envelope glycoprotein G of the Indiana serotype of vesicular stomatitis virus was modified not only by palmitylation, but also by myristylation, both occurring at the carboxy-terminal segment. When infected Chinese hamster ovary cells were grown in medium containing [3H]-myristate, the G protein and Ga2, the membrane-anchoring fragment containing about 71 amino acids, were labeled. This was shown by immunoprecipitation of cell lysates or extracellular fractions of infected cultures. Thin-layer chromatography of the fatty acid fraction released from G by hydrochloride hydrolysis showed that myristate, per se, was bound to G. The sensitivity of the fatty acid linkage to KOH/methanol indicated that [3H]-myristate was linked to the protein via ester or thioester bond(s). In contrast, the G protein of New Jersey serotype was not myristylated.
Chen
S S
SS
Department of Pediatrics, Harvard Medical School, Children's Hospital, Boston, MA 02115.
D000818:Animals; D002460:Cell Line; D002855:Chromatography, Thin Layer; D006224:Cricetinae; D005227:Fatty Acids / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D015531:Radioimmunoprecipitation Assay; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D018116:Vesiculovirus; D014759:Viral Envelope Proteins / Q000378:metabolism*
D005227:Fatty Acids; C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D009227:Myristic Acids; D014759:Viral Envelope Proteins; D019814:Myristic Acid