Laboratory of Molecular Biology, Department of Genetics and Evolution, Federal University of São Carlos, Rod: Washington Luis, Brazil.
Protein J. 2011 Aug;30(6):404-12. doi: 10.1007/s10930-011-9345-x.
Serine peptidase inhibitors (serpins) form a superfamily of proteins covering abroad spectrum of different biological functions. Here we describe the inhibitory characterization of leviserpin, the first serpin from the sugar cane weevil Sphenophorus levis. Leviserpin was able to inhibit bovine trypsin by the formation of the covalent complex serpin-peptidase, demonstrated by SDS-PAGE and mass spectroscopy analysis. We also have determined the cleavage site at the reactive center loop, by the analysis of the polypeptides released from de C-terminus of leviserpin. Moreover we investigated the mRNA expression of leviserpin in different stages of S. levis development. Thus the specificity of leviserpin, in addition with its mRNA coding being transcribed through all lifecycle of the insect, can suggest a possible role in defense mechanism by regulating the action of prophenoloxidase (proPO) activating enzyme.
丝氨酸蛋白酶抑制剂（serpins）构成了一个超家族的蛋白质，涵盖了广泛的不同生物学功能。在这里，我们描述了甘蔗象鼻虫 Sphenophorus levis 中第一个丝氨酸蛋白酶抑制剂 leviserpin 的抑制特性。Leviserpin 能够通过 SDS-PAGE 和质谱分析证实的丝氨酸蛋白酶-抑制剂共价复合物的形成来抑制牛胰蛋白酶。我们还通过分析从 leviserpin 的 C 末端释放的多肽，确定了活性中心环的切割位点。此外，我们研究了 leviserpin 在 S. levis 发育的不同阶段的 mRNA 表达。因此，leviserpin 的特异性及其 mRNA 编码在昆虫的整个生命周期中都被转录，可以暗示它在通过调节酚氧化酶原（proPO）激活酶的作用来调节防御机制方面的可能作用。
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