Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

FEBS Letters

Caamaño, Claudio A.¹  Zand, Robert¹ 

[1] Biophysics Research Division, Institute of Science and Technology and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-2099, USA

关键词: Myelin basic protein;    Cholera toxin;    Sequence homology;   

DOI  :  10.1016/0014-5793(89)80894-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown