Evolutionary Divergence in the Structure of Myelin Basic Protein: Comparison of Chondrichthye Basic Proteins with Those from Higher Vertebrates

• Published in: Journal of Neurochemistry
• Main Authors: Tai, F. L., Smith, Ross, Bernard, C. C. A., Hearn, M. W. T.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1986
• Subjects: antartic*
• Online Access: http://dx.doi.org/10.1111/j.1471-4159.1986.tb00617.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1471-4159.1986.tb00617.x; https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1471-4159.1986.tb00617.x

Abstract: A basic protein has been purified from the CNS myelin of the gummy shark ( Mustelus antarticus ). Electroblotting was used to examine the capacity of rabbit antisera raised against this electrophoretically pure protein to recognize myelin basic protein from higher vertebrates. The antisera bound to two shark proteins including the original polypeptide antigen and to chicken, bovine, and human myelin basic proteins. Thus, the shark protein appeared to possess antigenic determinants that have been retained through evolutionary divergence of these proteins. Whereas bovine basic protein caused experimental allergic encephalomyelitis in guinea pigs, animals that received injections of the shark protein showed neither clinical nor histological signs of this disease. However, tests for delayed‐type hypersensitivity and for Arthus reaction following injection with the shark protein revealed a T‐cell‐mediated response to this antigen and substantial cross‐reactivity with higher vertebrate basic proteins. Analysis of the amino acid composition of the shark protein, and comparison of its tryptic peptide map with that of the bovine protein, revealed substantial changes in the amino acid sequence. Although the shark protein has some antigenic determinants in common with the proteins from higher vertebrates, it appears that much of the structure differs.