Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein.
Recent reports that myelin basic protein (MBP) can be ADP-ribosylated and contains specific sites that bind GTP and GM1 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 less than 0.0007) and an 11 residue span (residues 31-41 in chol B and sequence 29-39 in hMBP, p less than 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 less than 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.
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Biophysics Research Division, University of Michigan, Ann Arbor 48109-2099.
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D000595:Amino Acid Sequence; D001483:Base Sequence; D002772:Cholera Toxin; D006801:Humans; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D004676:Myelin Basic Protein; D002772:Cholera Toxin