Autoimmune disease--pathogenesis through molecular mimicry at the tripeptide level.
Increasingly it is being discovered that short segments of proteins can provoke an immune response. Sequential determinants are as important as conformational determinants. It is the thesis of this paper that a string of three amino acid residues (a tripeptide) is antigenic when it is located on a large carrier, that is, when it is part of a protein. Conceptually this has great explanatory power in understanding (a) autoimmune phenomena (b) the intriguing finding that monoclonal antibodies which are supposed to be exquisitely specific cross-react with disparate, non-homologous proteins. Clinical syndromes such as the neuropathies of myeloma, hepatitis and multiple sclerosis are discussed in the light of this concept by computer analysis of the putative antigenic sites of myelin basic protein, hepatitis B and A proteins and measles peptides.
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D000956:Antigens, Viral / Q000276:immunology; D001327:Autoimmune Diseases / Q000276:immunology*; D003198:Computer Simulation; D003429:Cross Reactions; D000939:Epitopes / Q000276:immunology*; D035921:Hepatitis A Antigens; D006514:Hepatitis B Surface Antigens / Q000276:immunology; D006801:Humans; D009101:Multiple Myeloma / Q000276:immunology; D004676:Myelin Basic Protein / Q000276:immunology; D010455:Peptides / Q000276:immunology*; D012984:Software
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D000939:Epitopes; D035921:Hepatitis A Antigens; D006514:Hepatitis B Surface Antigens; D004676:Myelin Basic Protein; D010455:Peptides