Modification of tobacco mosaic virus by polyornithine and lecithin.
Combined action of polyornithine and lecithin modified tobacco mosaic virus (TMV) virions making them sensitive to ribonuclease (RNase), pronase or Triton X-100. Sedimentational analysis and examination of the fluorescence spectrum revealed that the reaction product obtained after RNase treatments of modified TMV was a three-component complex made of coat protein, polyornithine and lecithin. The minimum requirement for the modification was completely fulfilled by cetyltrimethylammonium bromide, suggesting that a positively charged nitrogen group and an alkyl group of moderate size, C10--18, are necessary components. These components react with the surface region of TMV which is considered to have an important role in connecting coat protein subunits in TMV virions.
D002593:Cetrimonium Compounds / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D010455:Peptides / Q000494:pharmacology*; D010713:Phosphatidylcholines / Q000494:pharmacology*; D011092:Polyethylene Glycols / Q000494:pharmacology; D011402:Pronase / Q000494:pharmacology; D012260:Ribonucleases / Q000494:pharmacology; D014027:Tobacco Mosaic Virus / Q000187:drug effects*; D014764:Viral Proteins / Q000378:metabolism; D014771:Virion / Q000187:drug effects
D002593:Cetrimonium Compounds; D010455:Peptides; D010713:Phosphatidylcholines; D014764:Viral Proteins; C008973:polyornithine; D011092:Polyethylene Glycols; D012260:Ribonucleases; D011402:Pronase