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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria
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Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria

机译：常春藤蛋白家族的结构和进化，革兰氏阴性细菌中意想不到的溶菌酶抑制剂

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摘要

Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherkhia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antily-sozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such. Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates.
机译：祖先杀菌系统的一部分，脊椎动物C型溶菌酶靶向细菌细胞壁的肽聚糖部分。我们报告了单独和与鸡蛋白溶菌酶复合的C型溶菌酶，大肠杆菌常春藤蛋白的蛋白质抑制剂的晶体结构。常春藤表现出新颖的折叠，其中突出的五残基环似乎对其抑制作用至关重要。此功能指导其他革兰氏阴性细菌中常春藤直系同源物的鉴定。还确定了与鸡蛋清溶菌酶复合的进化距离远的铜绿假单胞菌常春藤直系同源物的结构，并确认了其抗溶菌活性。常春藤表达保护多孔细胞壁大肠杆菌突变体免受溶菌酶的裂解作用，表明它是对先天脊椎动物免疫系统通透性作用的反应。因此。常春藤是许多革兰氏阴性细菌感染脊椎动物的致病因子。

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