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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural basis for conserved complement factor-like function in the antimalarial protein TEP1
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Structural basis for conserved complement factor-like function in the antimalarial protein TEP1

机译：抗疟蛋白TEP1中保守补体因子样功能的结构基础

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摘要

Thioester-containing proteins (TEPs) are a major component of the innate immune response of insects to invasion by bacteria and protozoa. TEPs form a distinct clade of a superfamily that includes the pan-protease inhibitors α_2-macroglobulins and vertebrate complement factors. The essential feature of these proteins is a sequestered thioester bond that, after cleavage in a protease-sensitive region of the protein, is activated and covalently binds to its target. Recently, TEP1 from the malarial vector Anopheles gambiae was shown to mediate recognition and killing of ookinetes rnfrom the malarial parasite Plasmodium berghei. a model for the human malarial parasite Plasmodium falciparum. Here, we present the crystal structure of the TEP1 isoform TEP1r. Although the overall protein fold of TEP1r resembles that of complement factor C3, the TEP1r domains are repositioned to stabilize the inactive conformation of the molecule (containing an intact thioester) in the absence of the anaphylotoxin domain, a central component of complement factors. The structure of TEP1 r provides a molecular basis for the differences between TEP1 alleles TEP1r and TEP1s. which correlate with resistance of A. gambiae to infection by P. berghei.
机译：含硫酯的蛋白质（TEP）是昆虫对细菌和原生动物入侵的先天免疫反应的主要组成部分。 TEP形成了一个超家族的独特分支，其中包括泛蛋白酶抑制剂α_2-巨球蛋白和脊椎动物补体因子。这些蛋白质的基本特征是螯合的硫酯键，在蛋白质的蛋白酶敏感区域切割后，该硫酯键被激活并与目标蛋白共价结合。最近，显示来自疟疾载体冈比亚按蚊的TEP1介导了对疟原虫伯氏疟原虫疟原虫的钩虫的识别和杀灭。人类疟原虫恶性疟原虫的模型。在这里，我们介绍了TEP1同工型TEP1r的晶体结构。尽管TEP1r的整体蛋白质折叠类似于补体因子C3的蛋白质折叠，但在缺少补体毒素的主要成分过敏毒素域的情况下，TEP1r结构域被重新定位以稳定分子的无活性构象（包含完整的硫酯）。 TEP1r的结构为TEP1等位基因TEP1r和TEP1s之间的差异提供了分子基础。与冈比亚土壤杆菌对伯氏疟原虫感染的抗性有关。

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