Change search
ReferencesLink to record
Permanent link

Direct link
Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells.
Umeå University, Faculty of Medicine, Molecular Biology (Faculty of Medicine). (Francis)
Umeå University, Faculty of Science and Technology, Molecular Biology (Faculty of Science and Technology). (Rosqvist)
Umeå University, Faculty of Science and Technology, Molecular Biology (Faculty of Science and Technology). (Francis)
Umeå University, Faculty of Science and Technology, Molecular Biology (Faculty of Science and Technology). (Francis)
2007 (English)In: Microbes and infection, ISSN 1286-4579, Vol. 9, no 2, 224-233 p.Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
2007. Vol. 9, no 2, 224-233 p.
Keyword [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
URN: urn:nbn:se:umu:diva-16668DOI: 10.1016/j.micinf.2006.11.010PubMedID: 17223369OAI: diva2:156341
Available from: 2007-10-08 Created: 2007-10-08 Last updated: 2010-03-03Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Liu, JunfaFrancis, Matthew S
By organisation
Molecular Biology (Faculty of Medicine)Molecular Biology (Faculty of Science and Technology)
In the same journal
Microbes and infection

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 57 hits
ReferencesLink to record
Permanent link

Direct link