Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface.
The mRNA coding for the structural proteins of Semliki Forest virus, the 26S RNA, was injected into Xenopus oocytes. Synthesis of the capsid protein and the three envelope glycoproteins E1, E2 and E2 was observed. The proteins, which are normally incorporated into the plasma membrane of infected cells, are transported to the surface of the oocytes. The transport of the membrane proteins takes place in the presence of tunicamycin. The results show that the proteins foreign to the oocyte reach their destination in the plasma membrane. Consequently, the mRNA contains the information for the transport and proteolytic cleavage of the polypeptides.
D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002213:Capsid / Q000096:biosynthesis; D002462:Cell Membrane / Q000378:metabolism; D005260:Female; D007163:Immunosorbent Techniques; D009865:Oocytes / Q000378:metabolism / Q000382:microbiology*; D012333:RNA, Messenger / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012672:Semliki forest virus / Q000235:genetics*; D014415:Tunicamycin / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000096:biosynthesis*; D014982:Xenopus laevis
D012333:RNA, Messenger; D012367:RNA, Viral; D014759:Viral Envelope Proteins; D014415:Tunicamycin