Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells |
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Authors: | Edqvist Petra J Aili Margareta Liu Junfa Francis Matthew S |
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Institution: | 1. Institute for Cellular Therapeutics, University of Louisville, Louisville, KY 40202, United States;2. Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40202, United States;3. Center for Predictive Medicine for Biodefense and Emerging Infectious Diseases, University of Louisville, Louisville, KY 40202, United States;1. Molecular Characterization of Foodborne Pathogens, US Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, 600 East Mermaid Lane, Wyndmoor, PA 19038, USA;2. Food Safety& Intervention Technologies Research Units, US Department of Agriculture, Agricultural Research Service, Eastern Regional Research Center, 600 East Mermaid Lane, Wyndmoor, PA 19038, USA;1. Department of Chemistry and Biochemistry, University of Missouri–Saint Louis, One University Boulevard, St. Louis, MO 63121, United States;2. Center for Nanoscience, University of Missouri–Saint Louis, One University Boulevard, St. Louis, MO 63121, United States;3. Department of Biochemistry and Molecular Biology, and Chemical Genomics Core Facility, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, United States;1. Department of Chemistry, University of Illinois at Chicago, 845 W. Taylor Street, Chicago, IL 60607, United States;2. Center for Pharmaceutical Biotechnology, University of Illinois at Chicago, Chicago, IL 60607, United States;3. Loyola University Medical Center, Maywood, IL 60153, United States |
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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. |
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