UMR203 Biologie Fonctionnelle Insectes et Interactions, IFR41, INRA, INSA-Lyon, F-69021 Villeurbanne, France.
J Insect Sci. 2007;7:1-10. doi: 10.1673/031.007.1201.
The aim of this work was to investigate both the biological activity of an entomotoxin, the pea albumin 1b (PA1b), and the presence or absence of its binding site within an array of insect species. The data obtained showed that insect sensitivity was not related to its taxonomic position. Moreover, PA1b was not toxic to several tested microorganisms. However, the binding site was found to be conserved among very different insects, displaying similar thermodynamic constants regardless of the in vivo species sensitivity. The binding site alone was, therefore, not sufficient for toxicity. One exception was the pea weevil, Bruchus pisorum, which was the only tested species without any detectable binding activity. These findings indicate that the binding site probably has an important endogenous function in insects and that adaptation to pea seeds resulted in the elimination of the toxin binding activity in two independent insect lineages. Other mechanisms are likely to interact with the toxin effects, although they are still largely unknown, but there is no evidence of any specific degradation of PA1b in the midgut of insects insensitive to the toxin, such as Drosophila melanogaster or Mamestra brassicae.
这项工作的目的是研究一种昆虫毒素——豌豆白蛋白 1b(PA1b)的生物学活性,以及其结合位点在一系列昆虫物种中的存在或缺失情况。所得数据表明,昆虫的敏感性与其分类地位无关。此外,PA1b 对几种测试的微生物没有毒性。然而,结合位点在非常不同的昆虫中被发现是保守的,无论体内物种的敏感性如何,都表现出相似的热力学常数。因此,仅仅结合位点本身对于毒性来说是不够的。一个例外是豌豆象,Bruchus pisorum,它是唯一没有任何可检测到的结合活性的测试物种。这些发现表明,结合位点可能在昆虫中有重要的内源性功能,并且对豌豆种子的适应导致了两种独立的昆虫谱系中毒素结合活性的消除。虽然其他机制可能与毒素的作用相互作用,但它们在很大程度上仍然未知,但没有证据表明在对毒素不敏感的昆虫(如黑腹果蝇或菜粉蝶)的中肠中,PA1b 有任何特定的降解。