Characterization of the AfaD-like family of invasins encoded by pathogenic Escherichia coli associated with intestinal and extra-intestinal infections
Characterization of the AfaD-like family of invasins encoded by pathogenic Escherichia coli associated with intestinal and extra-intestinal infections
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DOI：
10.1016/s0014-5793(00)01898-6
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发表时间：
2000-08-18
期刊：
影响因子：
3.5
通讯作者：
Le Bouguénec, C
中科院分区：
文献类型：
--
作者：
Garcia, MI;Jouve, M;Le Bouguénec, C
由afa-3基因簇编码的无菌毛粘附鞘由两种在细菌-Hela细胞相互作用中具有不同作用的蛋白质组成。AfaE是粘附所必需的，AfaD是内化所必需的。在这项研究中，我们发现AfaD侵袭素在人afa表达菌株中在结构和功能上是保守的，与大肠杆菌分离株的AfaE亚型和临床来源无关。肠聚集性大肠杆菌AggB蛋白的表达。coli中也发现了一种与AfaD相关的侵袭素。这些数据表明，AfaD是致病性大肠杆菌中粘附相关操纵子编码的侵袭素家族的原型。杆菌(C)2000年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
The afimbrial adhesive sheath, encoded by the afa-3 gene cluster, is composed of two proteins with different roles in bacterium-Hela cell interactions. AfaE is required for adhesion and AfaD for internalization, In this study, we found that the AfaD invasin was structurally and functionally conserved among human afa-expressing strains, independently of AfaE subtype and clinical origin of the Escherichia coli isolate. The AggB protein from enteroaggregative E. coli was also found to be an AfaD-related invasin. These data suggest that AfaD is the prototype of a family of invasins encoded by adhesion-associated operons in pathogenic E. coli. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.