Einfluß der Tertiärstruktur auf die serologischen Eigenschaften des Tabakmosaikvirus

Abstract

Four derivatives of tobacco mosaic virus protein have been prepared by substituting different groups of the amino acid sidechains. The influence of the substituents on the reformation of the native protein structure has been studied by electron microscopy (reformation of typical protein rods) and by serological methods (precipitation with anti TMV serum). The results indicate that the reaction with anti TMV serum is not dependent on the correct quaternary structure of the virus, but rather on the tertiary structure of the protein subunits of the virus. There is no evidence for specific antibodies against isolated amino acid sequences of the polypeptide chain of TMV. Further evidence is provided by serological investigations of virus protein partially degradated by enzymes.