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Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein
Author(s) -
Caamaño Claudio A.,
Zand Robert
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80894-4
Subject(s) - cholera toxin , homologous chromosome , peptide , toxin , vibrio cholerae , myelin basic protein , chemistry , protein subunit , biology , myelin , biochemistry , genetics , microbiology and biotechnology , bacteria , gene , central nervous system , neuroscience
Recent reports that myelin basic protein (MBP) can be ADP‐ribosylated and contains specific sites that bind GTP and G M1 ganglioside, have suggested an analogy to the properties of cholera toxin. Comparisons of pairs of sequences between these two proteins yielded two regions of homology between MBP and the cholera toxin B (chol B) subunit, and one region of homology with the cholera toxin A (chol A) subunit. The matching sites within chol B consisted of a 17 amino acid residue sequence (residues 30–46 in chol B and residues 102–118 in human‐MBP, hMBP, p <0.0007) and an 11 residue span (residues 31–41 in chol B and sequence 29–39 in hMBP, p <0.0004). The homologous site within chol A corresponded to an 11 residue span (residues 130–140 in chol A and 67–77 in hMBP sequence, p <0.00007). Since portions of the cholera toxin sequence are virtually identical to sections of the sequence in E. coli toxin, the homology is also valid for the same sequences in this toxin. The highly antigenic behavior of MBP that is related to the induction of experimental allergic encephalomyelitis may be paralleled by comparable neural pathology from the homologous regions of cholera toxin.