Charpentier I, Pillet L, Karlsson E, Couderc J, Ménez A
Département de Biologie, Protéines CEN Saclay, Gif-sur Yvette, France.
J Mol Recognit. 1990 Apr;3(2):74-81. doi: 10.1002/jmr.300030204.
The present paper reports the preparation and characterization of two neutralizing monoclonal antibodies (Mabs), called MST1 and MST2, which bind at the central loop of a long-chain neurotoxin from cobra venom. The central loop is a critical region for the binding of the toxin to the nicotinic acetylcholine receptor. Some of the residues incorporated in the epitopes recognized by MST1 and MST2 have been identified on the basis of competition experiments using a set of 'chemical mutants' of the toxin. We show that MST1 and MST2 bind at the base and at the tip of the central loop of the toxin, respectively, however, only MST2 actually overlaps the acetylcholine receptor binding site. Accordingly, only MST2 is capable of recognizing all homologous toxins so far examined. MST2, therefore, mimicks, at least partially, the site by which the nicotinic acetylcholine receptor recognizes a long-chain neurotoxin.
本文报道了两种中和性单克隆抗体（MST1和MST2）的制备与特性，这两种抗体与眼镜蛇毒长链神经毒素的中央环结合。中央环是毒素与烟碱型乙酰胆碱受体结合的关键区域。基于使用该毒素的一组“化学突变体”进行的竞争实验，已鉴定出MST1和MST2识别的表位中包含的一些残基。我们发现，MST1和MST2分别结合在毒素中央环的基部和顶端，然而，只有MST2实际与乙酰胆碱受体结合位点重叠。因此，到目前为止，只有MST2能够识别所有检测的同源毒素。所以，MST2至少部分模拟了烟碱型乙酰胆碱受体识别长链神经毒素的位点。
