Publications
2013
Kobayashi Taira, Ogawa Michinaga, Sanada Takahito, Mimuro Hitomi, Kim Minsoo, Ashida Hiroshi, Akakura Reiko, Yoshida Mitsutaka, Kawalec Magdalena, Reichhart Jean-Marc, Mizushima Tsunehiro, Sasakawa Chihiro
The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection Article de journal
Dans: Cell Host Microbe, vol. 13, no. 5, p. 570–583, 2013, ISSN: 1934-6069.
Résumé | Liens | BibTeX | Étiquettes: Animal, Animals, Bacillary, Bacterial, Bacterial Proteins, Caspases, Cell Death, Cell Line, Disease Models, DNA, Dysentery, Enzyme Inhibitors, Epithelial Cells, Escherichia coli, Gene Knockout Techniques, Guinea Pigs, Host-Pathogen Interactions, Humans, Initiator, M3i, Protein Binding, Protein Interaction Mapping, reichhart, Salmonella typhimurium, Sequence Analysis, Shigella flexneri, Virulence Factors
@article{kobayashi_shigella_2013,
title = {The Shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection},
author = {Taira Kobayashi and Michinaga Ogawa and Takahito Sanada and Hitomi Mimuro and Minsoo Kim and Hiroshi Ashida and Reiko Akakura and Mitsutaka Yoshida and Magdalena Kawalec and Jean-Marc Reichhart and Tsunehiro Mizushima and Chihiro Sasakawa},
doi = {10.1016/j.chom.2013.04.012},
issn = {1934-6069},
year = {2013},
date = {2013-05-01},
journal = {Cell Host Microbe},
volume = {13},
number = {5},
pages = {570--583},
abstract = {Caspase-mediated inflammatory cell death acts as an intrinsic defense mechanism against infection. Bacterial pathogens deploy countermeasures against inflammatory cell death, but the mechanisms by which they do this remain largely unclear. In a screen for Shigella flexneri effectors that regulate cell death during infection, we discovered that Shigella infection induced acute inflammatory, caspase-4-dependent epithelial cell death, which is counteracted by the bacterial OspC3 effector. OspC3 interacts with the caspase-4-p19 subunit and inhibits its activation by preventing caspase-4-p19 and caspase-4-p10 heterodimerization by depositing the conserved OspC3 X1-Y-X₂-D-X₃ motif at the putative catalytic pocket of caspase-4. Infection of guinea pigs with a Shigella ospC3-deficient mutant resulted in enhanced inflammatory cell death and associated symptoms, correlating with decreased bacterial burdens. Salmonella Typhimurium and enteropathogenic Escherichia coli infection also induced caspase-4-dependent epithelial death. These findings highlight the importance of caspase-4-dependent innate immune responses and demonstrate that Shigella delivers a caspase-4-specific inhibitor to delay epithelial cell death and promote infection.},
keywords = {Animal, Animals, Bacillary, Bacterial, Bacterial Proteins, Caspases, Cell Death, Cell Line, Disease Models, DNA, Dysentery, Enzyme Inhibitors, Epithelial Cells, Escherichia coli, Gene Knockout Techniques, Guinea Pigs, Host-Pathogen Interactions, Humans, Initiator, M3i, Protein Binding, Protein Interaction Mapping, reichhart, Salmonella typhimurium, Sequence Analysis, Shigella flexneri, Virulence Factors},
pubstate = {published},
tppubtype = {article}
}
2011
Ogawa Michinaga, Yoshikawa Yuko, Kobayashi Taira, Mimuro Hitomi, Fukumatsu Makoto, Kiga Kotaro, Piao Zhenzi, Ashida Hiroshi, Yoshida Mitsutaka, Kakuta Shigeru, Koyama Tomohiro, Goto Yoshiyuki, Nagatake Takahiro, Nagai Shinya, Kiyono Hiroshi, Kawalec Magdalena, Reichhart Jean-Marc, Sasakawa Chihiro
A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens Article de journal
Dans: Cell Host Microbe, vol. 9, no. 5, p. 376–389, 2011, ISSN: 1934-6069.
Résumé | Liens | BibTeX | Étiquettes: Animals, Autophagy, Biological, Cells, Cultured, M3i, Membrane Proteins, Mice, Microtubule-Associated Proteins, Models, Phagosomes, Protein Interaction Mapping, reichhart, Shigella, Two-Hybrid System Techniques
@article{ogawa_tecpr1-dependent_2011,
title = {A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens},
author = {Michinaga Ogawa and Yuko Yoshikawa and Taira Kobayashi and Hitomi Mimuro and Makoto Fukumatsu and Kotaro Kiga and Zhenzi Piao and Hiroshi Ashida and Mitsutaka Yoshida and Shigeru Kakuta and Tomohiro Koyama and Yoshiyuki Goto and Takahiro Nagatake and Shinya Nagai and Hiroshi Kiyono and Magdalena Kawalec and Jean-Marc Reichhart and Chihiro Sasakawa},
doi = {10.1016/j.chom.2011.04.010},
issn = {1934-6069},
year = {2011},
date = {2011-05-01},
journal = {Cell Host Microbe},
volume = {9},
number = {5},
pages = {376--389},
abstract = {Selective autophagy of bacterial pathogens represents a host innate immune mechanism. Selective autophagy has been characterized on the basis of distinct cargo receptors but the mechanisms by which different cargo receptors are targeted for autophagic degradation remain unclear. In this study we identified a highly conserved Tectonin domain-containing protein, Tecpr1, as an Atg5 binding partner that colocalized with Atg5 at Shigella-containing phagophores. Tecpr1 activity is necessary for efficient autophagic targeting of bacteria, but has no effect on rapamycin- or starvation-induced canonical autophagy. Tecpr1 interacts with WIPI-2, a yeast Atg18 homolog and PI(3)P-interacting protein required for phagophore formation, and they colocalize to phagophores. Although Tecpr1-deficient mice appear normal, Tecpr1-deficient MEFs were defective for selective autophagy and supported increased intracellular multiplication of Shigella. Further, depolarized mitochondria and misfolded protein aggregates accumulated in the Tecpr1-knockout MEFs. Thus, we identify a Tecpr1-dependent pathway as important in targeting bacterial pathogens for selective autophagy.},
keywords = {Animals, Autophagy, Biological, Cells, Cultured, M3i, Membrane Proteins, Mice, Microtubule-Associated Proteins, Models, Phagosomes, Protein Interaction Mapping, reichhart, Shigella, Two-Hybrid System Techniques},
pubstate = {published},
tppubtype = {article}
}