Document Detail

Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells.
MedLine Citation:
PMID:  17223369     Owner:  NLM     Status:  MEDLINE    
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.
Petra J Edqvist; Margareta Aili; Junfa Liu; Matthew S Francis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-12-18
Journal Detail:
Title:  Microbes and infection / Institut Pasteur     Volume:  9     ISSN:  1286-4579     ISO Abbreviation:  Microbes Infect.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-02-16     Completed Date:  2007-08-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100883508     Medline TA:  Microbes Infect     Country:  France    
Other Details:
Languages:  eng     Pagination:  224-33     Citation Subset:  IM    
Department of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
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MeSH Terms
Bacterial Outer Membrane Proteins / biosynthesis*
Bacterial Proteins / biosynthesis,  genetics,  physiology*
Hela Cells
Molecular Chaperones / genetics,  physiology*
Point Mutation
Pore Forming Cytotoxic Proteins / biosynthesis
Protein Binding
Protein Transport / genetics
Virulence Factors / metabolism*
Yersinia pseudotuberculosis / genetics,  metabolism,  pathogenicity*
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Bacterial Proteins; 0/Molecular Chaperones; 0/Pore Forming Cytotoxic Proteins; 0/SycD protein, bacteria; 0/Virulence Factors; 0/YopB protein, Yersinia; 0/YopD protein, Yersinia

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