The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.
The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.
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SopB(沙门氏菌的毒力因子)的 N 末端结构域的结构组织取决于其蛋白质伙伴的性质。
DOI:
10.1016/j.bbapap.2013.09.014
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发表时间:
2013
期刊:
影响因子:
--
通讯作者:
C. Bompard
中科院分区:
文献类型:
--
作者:
P. Roblin;Pierre Lebrun;P. Rucktooa;F. Dewitte;Zoé Lens;V. Receveur;V. Raussens;V. Villeret;C. Bompard
The TTSS is used bySalmonellaand many bacterial pathogens to inject virulence factors directly into the cytoplasm of target eukaryotic cells. Once translocated these so-called effector proteins hijack a vast array of crucial cellular functions to the benefit of the bacteria. In the bacterial cytoplasm, some effectors are stabilized and maintained in a secretion competent state by interaction with specific type III chaperones. In this work we studied the conformation of the Chaperone Binding Domain of the effector namedSalmonellaOuter protein B (SopB) alone and in complex with its cognate chaperone SigE by a combination of biochemical, biophysical and structural approaches. Our results show that the N-terminus part of SopB is mainly composed by α-helices and unfolded regions whose organization/stabilization depends on their interaction with the different partners. This suggests that the partially unfolded state of this N-terminal region, which confers the adaptability of the effector to bind very different partners during the infection cycle, allows the bacteria to modulate numerous host cells functions limiting the number of translocated effectors.
影响因子:
16
作者:
Birtalan, SC;Phillips, RM;Ghosh, P
通讯作者:
Ghosh, P
影响因子:
6.8
作者:
Wright, Peter E.;Dyson, H. Jane
通讯作者:
Dyson, H. Jane
影响因子:
16
作者:
Lilic, M;Vujanac, M;Stebbins, CE
通讯作者:
Stebbins, CE