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

机译:霍乱毒素a和B亚基中的同源序列到髓鞘碱性蛋白中的肽结构域

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摘要

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, pppE. 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.
机译:最近的报道表明髓磷脂碱性蛋白(MBP)可以被ADP核糖基化,并包含结合GTP和GM1神经节苷脂的特定位点,这暗示了霍乱毒素的特性。这两种蛋白质之间的序列对比较产生了MBP和霍乱毒素B(chol B)亚基之间的两个同源区域,以及一个与霍乱毒素A(chol A)亚基的同源性区域。 chol B中的匹配位点由17个氨基酸残基序列组成(chol B中的30-46位残基和人MBP,hMBP,pppE。coli毒素中的102-118位残基,该同源性也适用于该序列中的相同序列与诱导实验性变应性脑脊髓炎有关的MBP的高度抗原性行为可能与霍乱毒素同源区域的可比神经病理学平行。

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