Influence of local structure on the location of antigenic determinants in tobacco mosaic virus protein.
Early work on protein antigenicity led to the common belief that proteins possess a finite number of antigenic determinants located in accessible regions of the molecule's surface. This view is now changing. As a result of extensive studies, seven continuous epitopes have been located on tobacco mosaic virus (TMV) protein by measuring the antigenic activity of short peptides with anti-protein antibodies. The structure of the viral protein has been refined in Cambridge, enabling the Strasbourg workers to correlate the position of these epitopes with regions of high segmental mobility in the protein. Surface accessibility is not a sufficient condition for antigenicity, because six short peptides corresponding to accessible regions of the protein possess no antigenic activity. Recent work in Strasbourg shows that when longer peptides of TMV protein are used, more antigenic determinants are found and these lie in more structured regions of the protein (e.g. helices). In these cases the longer peptide may be folding up in solution to mimic part of the native structure.
D000956:Antigens, Viral; D003429:Cross Reactions; D003461:Crystallography; D000939:Epitopes; D010455:Peptides / Q000276:immunology; D011487:Protein Conformation; D014027:Tobacco Mosaic Virus / Q000276:immunology*; D014764:Viral Proteins / Q000276:immunology*
D000956:Antigens, Viral; D000939:Epitopes; D010455:Peptides; D014764:Viral Proteins