Intermediate filaments enable pathogen docking to trigger type 3 effector translocation

Type 3 secretion systems (T3SSs) of bacterial pathogens translocate bacterial effector proteins that mediate disease into the eukaryotic cytosol. Effectors traverse the plasma membrane through a translocon pore formed by T3SS proteins. In a genome-wide selection, we identified the intermediate filam...

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Vydané v:Nature microbiology Ročník 1; číslo 4; s. 16025
Hlavní autori: Russo, Brian C., Stamm, Luisa M., Raaben, Matthijs, Kim, Caleb M., Kahoud, Emily, Robinson, Lindsey R., Bose, Sayantan, Queiroz, Ana L., Herrera, Bobby Brooke, Baxt, Leigh A., Mor-Vaknin, Nirit, Fu, Yang, Molina, Gabriel, Markovitz, David M., Whelan, Sean P., Goldberg, Marcia B.
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: London Nature Publishing Group UK 07.03.2016
Nature Publishing Group
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Animals
Antigens, Bacterial - metabolism
Bacterial Adhesion
Biomedical and Life Sciences
C-Terminus
Cell Line
Cytosol
Filaments
Genomes
Host-Pathogen Interactions
Humans
Infectious Diseases
Intermediate filaments
Intestine
Keratin
Keratin-18 - metabolism
Life Sciences
Medical Microbiology
Mice
Microbiology
Parasitology
Pathogens
Protein Binding
Protein Transport
Pseudotuberculosis
Salmonella typhimurium - physiology
Secretion
Shigella flexneri - physiology
Type III Secretion Systems - metabolism
Vimentin
Vimentin - metabolism
Virology
Virulence Factors - metabolism
Yersinia pseudotuberculosis - physiology
ISSN:2058-5276, 2058-5276
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Shrnutí:Type 3 secretion systems (T3SSs) of bacterial pathogens translocate bacterial effector proteins that mediate disease into the eukaryotic cytosol. Effectors traverse the plasma membrane through a translocon pore formed by T3SS proteins. In a genome-wide selection, we identified the intermediate filament vimentin as required for infection by the T3SS-dependent pathogen S. flexneri . We found that vimentin is required for efficient T3SS translocation of effectors by S. flexneri and other pathogens that use T3SS, Salmonella enterica serovar Typhimurium and Yersinia pseudotuberculosis. Vimentin and the intestinal epithelial intermediate filament keratin 18 interact with the C-terminus of the Shigella translocon pore protein IpaC. Vimentin and its interaction with IpaC are dispensable for pore formation, but are required for stable docking of S. flexneri to cells; moreover, stable docking triggers effector secretion. These findings establish that stable docking of the bacterium specifically requires intermediate filaments, is a process distinct from pore formation, and is a prerequisite for effector secretion. Binding of type 3 secretion system translocons to host intermediate filaments mediate Shigella , Salmonella and Yersinia docking and facilitate effector translocation.
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Current Affiliations: Liver Diseases Therapeutic Area, Gilead Sciences, Foster City, CA 94404, USA
Current Affiliations: Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA
Current Affiliations: Netherlands Cancer Institute, 1066 CX, Amsterdam, NL
Current Affiliations: Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, MA 02114, USA
ISSN:2058-5276
2058-5276
DOI:10.1038/nmicrobiol.2016.25