A tentative model of formation of structural proteins of tick-borne encephalitis virus (flavivirus).
The time course of tick-borne encephalitis virus cell-free protein synthesis was studied by using either [35S]-methionine or formyl[35S]methionyl-tRNAMet/f as substrates, and the [35S]methionine-labelled products were compared by fingerprinting tryptic peptides. An intermediate in the protein processing, the polypeptide doublet p36/33, was characterized and a tentative model for flavivirus structural protein synthesis and processing was proposed.
D000595:Amino Acid Sequence; D004669:Encephalitis Viruses, Tick-Borne / Q000378:metabolism*; D008954:Models, Biological; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D012358:RNA, Transfer, Met; D013462:Sulfur Radioisotopes; D014764:Viral Proteins / Q000096:biosynthesis*; D015678:Viral Structural Proteins
D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; D013462:Sulfur Radioisotopes; D014764:Viral Proteins; D015678:Viral Structural Proteins; C024988:tRNA, formylmethionine-