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• W1975831923 endingPage "233" @default.
• W1975831923 startingPage "224" @default.
• W1975831923 abstract "Pathogenic Yersinia sp. utilise a common type III secretion system to translocate several anti-host Yop effectors into the cytosol of target eukaryotic cells. The secreted YopB and YopD translocator proteins are essential for this process, forming pores in biological membranes through which the effectors are thought to gain access to the cell interior. The non-secreted cognate chaperone, LcrH, also plays an important role by ensuring pre-secretory stabilisation and efficient secretion of YopB and YopD. This suggests that LcrH-regulated secretion of the translocators could be used by Yersinia to control effector translocation levels. We collected several LcrH mutants impaired in chaperone activity. These poorly bound, stabilised and/or secreted YopB and YopD in vitro. However, these mutants generally maintained stable substrates during a HeLa cell infection and these infected cells were intoxicated by translocated effectors. Surprisingly, this occurred in the absence of detectable YopB- and YopD-dependent pores in eukaryotic membranes. A functional type III translocon must therefore only require minuscule amounts of secreted translocator proteins. Based on these observations, LcrH dependent control of translocation via regulated YopB and YopD secretion would need to be exquisitely tight." @default.
• W1975831923 created "2016-06-24" @default.
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• W1975831923 creator A5056408892 @default.
• W1975831923 date "2007-02-01" @default.
• W1975831923 modified "2023-10-06" @default.
• W1975831923 title "Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells" @default.
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• W1975831923 doi "https://doi.org/10.1016/j.micinf.2006.11.010" @default.
• W1975831923 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17223369" @default.
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