Mansuelle P, Martin M F, Rochat H, Granier C
Centre National de la Recherche Scientifique UA 1455, Faculté de Médecine, Secteur Nord, Marseille, France.
Nat Toxins. 1992;1(1):61-9. doi: 10.1002/nt.2620010112.
The complete amino acid sequence (64 residues) of the AaH IV toxin from the scorpion Androctonus australis Hector was determined by automated Edman degradation and was compared with the sequences of other Androctonus toxins. AaH IV was also tested by radioimmunoassay for binding to antisera raised against other toxins of the same species. The results indicated that AaH IV shares some of the antigenic properties of AaH I and AaH III toxins, but does not cross-react with anti-AaH II antibodies. The structural basis for the observed antigenic relationships can be found in the high degree of homology displayed by AaH IV with regard to AaH I and III, the changes in amino acid residues equally affecting regions included or excluded from the main predicted antigenic sites of AaH IV. The lower biological potency of AaH IV is presumably the result of some of the sequence differences. In particular, substitution affecting the charge and bulkiness of residue 61 could account for the poor receptor binding and consequential weak toxic properties of this molecule.
通过自动埃德曼降解法测定了来自澳大利亚杀人蝎（Androctonus australis Hector）的AaH IV毒素的完整氨基酸序列（64个残基），并将其与其他杀人蝎毒素的序列进行了比较。还通过放射免疫分析法检测了AaH IV与针对同一物种其他毒素产生的抗血清的结合情况。结果表明，AaH IV具有AaH I和AaH III毒素的一些抗原特性，但不与抗AaH II抗体发生交叉反应。观察到的抗原关系的结构基础可以在AaH IV与AaH I和III所显示的高度同源性中找到，氨基酸残基的变化同样影响AaH IV主要预测抗原位点所包含或排除的区域。AaH IV较低的生物活性可能是某些序列差异的结果。特别是，影响第61位残基电荷和体积的取代可能导致该分子受体结合不良以及相应的弱毒性。
