Functional dissection of SseF, a membrane-integral effector protein of intracellular Salmonella enterica.

Functional dissection of SseF, a membrane-integral effector protein of intracellular Salmonella enterica.
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DOI:
10.1371/journal.pone.0035004
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Hensel M
Hensel M
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Müller P;Chikkaballi D;Hensel M

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在细胞内生活期间,细菌病原体肠道沙门氏菌通过SPI 2编码的III型分泌系统转运效应蛋白的复杂混合物。效应物共同修饰宿主细胞中的内体系统和囊泡转运。SseF和SseG是由沙门氏菌致病性岛2内的基因编码的两种效应物,并且这两种效应物与内体膜和微管相关,并且参与沙门氏菌诱导的细丝的形成。我们先前的缺失分析确定了效应子功能所需的SseF蛋白结构域。在这里,我们提出了一个详细的突变分析,确定一个短的疏水基序的功能至关重要。我们证明,SseF和SseG仍然是功能性的,如果易位作为一个单一的融合蛋白,但也介导效应功能,如果易位在细胞共感染sseF和sseG菌株。SseF在易位到宿主细胞后具有整合膜蛋白的特征。
During intracellular life, the bacterial pathogen Salmonella enterica translocates a complex cocktail of effector proteins by means of the SPI2-encoded type III secretions system. The effectors jointly modify the endosomal system and vesicular transport in host cells. SseF and SseG are two effectors encoded by genes within Salmonella Pathogenicity Island 2 and both effector associate with endosomal membranes and microtubules and are involved in the formation of Salmonella-induced filaments. Our previous deletional analyses identified protein domains of SseF required for the effector function. Here we present a detailed mutational analysis that identifies a short hydrophobic motif as functionally essential. We demonstrate that SseF and SseG are still functional if translocated as a single fusion protein, but also mediate effector function if translocated in cells co-infected with sseF and sseG strains. SseF has characteristics of an integral membrane protein after translocation into host cells.
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