The giant adhesin SiiE of Salmonella enterica.

The giant adhesin SiiE of Salmonella enterica.
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DOI:
10.3390/molecules20011134
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发表时间:
2015-01-12
期刊:
Molecules (Basel, Switzerland)
影响因子:
--
通讯作者:
Hensel M
Hensel M
中科院分区:
其他
文献类型:
--
作者:
Barlag B;Hensel M

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肠道沙门氏菌是一种革兰氏阴性的食源性病原体,其定植于肠道并侵入肠细胞。极化细胞的侵袭依赖于SPI 1编码的III型分泌系统(T3 SS)和SPI 4编码的I型分泌系统(T1 SS)。这种T1 SS的底物是非菌毛巨粘附素SiiE。SiiE是沙门氏菌蛋白质组中最大的蛋白质,大小为595 kDa,由53个重复的细菌免疫球蛋白(BIg)结构域组成,每个结构域含有几个保守残基。如已知的其它T1 SS底物,例如E. ColiHlyA中,BIg结构域内保守D残基结合的Ca 2+离子稳定蛋白并促进分泌。粘附素SiiE介导与宿主细胞的第一次接触,从而定位SPI 1-T3 SS以启动效应蛋白混合物的易位。这导致肌动蛋白重塑、膜皱褶形成和细菌内化。SiiE以凝集素样方式结合宿主细胞顶端膜。GlcNAc和α2-3连接的含唾液酸结构是SiiE的配体。由于SiiE显示重复的结构域架构,我们提出了一个拉链样的结合介导的每个单独的BIG结构域。本文就SPI 4-T1 SS和巨噬细胞粘附素SiiE的特性作一综述。
Salmonella enterica is a Gram-negative, food-borne pathogen, which colonizes the intestinal tract and invades enterocytes. Invasion of polarized cells depends on the SPI1-encoded type III secretion system (T3SS) and the SPI4-encoded type I secretion system (T1SS). The substrate of this T1SS is the non-fimbrial giant adhesin SiiE. With a size of 595 kDa, SiiE is the largest protein of the Salmonella proteome and consists of 53 repetitive bacterial immunoglobulin (BIg) domains, each containing several conserved residues. As known for other T1SS substrates, such as E. coli HlyA, Ca2+ ions bound by conserved D residues within the BIg domains stabilize the protein and facilitate secretion. The adhesin SiiE mediates the first contact to the host cell and thereby positions the SPI1-T3SS to initiate the translocation of a cocktail of effector proteins. This leads to actin remodeling, membrane ruffle formation and bacterial internalization. SiiE binds to host cell apical membranes in a lectin-like manner. GlcNAc and α2–3 linked sialic acid-containing structures are ligands of SiiE. Since SiiE shows repetitive domain architecture, we propose a zipper-like binding mediated by each individual BIg domain. In this review, we discuss the characteristics of the SPI4-T1SS and the giant adhesin SiiE.
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