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Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells.
Umeå universitet, Medicinsk fakultet, Molekylärbiologi (Medicinska fakulteten). (Francis)
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Molekylärbiologi (Teknisk-naturvetenskaplig fakultet). (Rosqvist)
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Molekylärbiologi (Teknisk-naturvetenskaplig fakultet). (Francis)
Umeå universitet, Teknisk-naturvetenskaplig fakultet, Molekylärbiologi (Teknisk-naturvetenskaplig fakultet). (Francis)
2007 (engelsk)Inngår i: Microbes and infection, ISSN 1286-4579, E-ISSN 1769-714X, Vol. 9, nr 2, s. 224-233Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
2007. Vol. 9, nr 2, s. 224-233
Emneord [en]
Bacterial Outer Membrane Proteins/*biosynthesis, Bacterial Proteins/biosynthesis/genetics/*physiology, Hela Cells, Humans, Molecular Chaperones/genetics/*physiology, Mutagenesis, Point Mutation, Pore Forming Cytotoxic Proteins/biosynthesis, Protein Binding, Protein Transport/genetics, Virulence Factors/*metabolism, Yersinia pseudotuberculosis/genetics/metabolism/*pathogenicity
Identifikatorer
URN: urn:nbn:se:umu:diva-16668DOI: 10.1016/j.micinf.2006.11.010PubMedID: 17223369OAI: oai:DiVA.org:umu-16668DiVA, id: diva2:156341
Tilgjengelig fra: 2007-10-08 Laget: 2007-10-08 Sist oppdatert: 2018-06-09bibliografisk kontrollert

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