Protein synthesis in Semliki Forest virus-infected cells is not controlled by permeability changes.
The uptake of the GTP analogue guanylyl(beta,gamma-methylene)diphosphonate (GppCH2p) is the same in Semliki Forest virus (SFV)-infected BHK cells as in mock-infected cells, in spite of the fact that protein synthesis is inhibited by GppCH2p more markedly in SFV-infected cells than in control cells. A possible explanation for this difference is that infected cells have a lower concentration of GTP and a lower ratio of GTP:GDP than uninfected cells, and the analogue may thus be a more effective competitive inhibitor of translation. We conclude that in this system, the difference between infected and uninfected cells lies not at the plasma membrane but within the cytoplasm.
D000818:Animals; D002460:Cell Line; D002463:Cell Membrane Permeability; D006224:Cricetinae; D004164:Diphosphonates / Q000378:metabolism* / Q000494:pharmacology; D006150:Guanine Nucleotides / Q000378:metabolism*; D006157:Guanosine Monophosphate / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000378:metabolism / Q000031:analogs & derivatives; D008757:Methylglucosides / Q000378:metabolism; D014176:Protein Biosynthesis; D012672:Semliki forest virus / Q000502:physiology*
D004164:Diphosphonates; D006150:Guanine Nucleotides; D008757:Methylglucosides; C004805:5'-guanylylmethylenebisphosphonate; C027020:methylglucoside; D006157:Guanosine Monophosphate; D006160:Guanosine Triphosphate