T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome.
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| Autores principales: | , , , , |
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| Formato: | Artículo científico |
| Lenguaje: | en |
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eLife
2025
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| _version_ | 1868266242353135618 |
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| author | Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li |
| author_facet | Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li |
| collection | PubMed - marine biology |
| contents | T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome. Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li Pyroptosis Inflammasomes Type III Secretion Systems Calcium-Binding Proteins CARD Signaling Adaptor Proteins Neuronal Apoptosis-Inhibitory Protein Humans Edwardsiella tarda Apoptosis Regulatory Proteins Animals Bacterial Proteins Mice Host-Pathogen Interactions Type III secretion system (T3SS) is a virulence apparatus existing in many bacterial pathogens. Structurally, T3SS consists of the base, needle, tip, and translocon. The NLRC4 inflammasome is the major receptor for T3SS needle and basal rod proteins. Whether other T3SS components are recognized by NLRC4 is unclear. In this study, using as a model intracellular pathogen, we examined T3SS-inflammasome interaction and its effect on cell death. induced pyroptosis in a manner that required the bacterial translocon and the host inflammasome proteins of NLRC4, NLRP3, ASC, and caspase 1/4. The translocon protein EseB triggered NLRC4/NAIP-mediated pyroptosis by binding NAIP via its C-terminal region, particularly the terminal 6 residues (T6R). EseB homologs exist widely in T3SS-positive bacteria and share high identities in T6R. Like EseB, all of the representatives of the EseB homologs exhibited T6R-dependent NLRC4 activation ability. Together these results revealed the function and molecular mechanism of EseB to induce host cell pyroptosis and suggested a highly conserved inflammasome-activation mechanism of T3SS translocon in bacterial pathogens. |
| format | Artículo científico |
| id | pubmed_39951384 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | eLife |
| record_format | pubmed |
| spellingShingle | T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome. Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li Pyroptosis Inflammasomes Type III Secretion Systems Calcium-Binding Proteins CARD Signaling Adaptor Proteins Neuronal Apoptosis-Inhibitory Protein Humans Edwardsiella tarda Apoptosis Regulatory Proteins Animals Bacterial Proteins Mice Host-Pathogen Interactions T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome. Zhao, Yan Zhu, Hanshuo Li, Jinqian Xu, Hang Sun, Li Pyroptosis Inflammasomes Type III Secretion Systems Calcium-Binding Proteins CARD Signaling Adaptor Proteins Neuronal Apoptosis-Inhibitory Protein Humans Edwardsiella tarda Apoptosis Regulatory Proteins Animals Bacterial Proteins Mice Host-Pathogen Interactions Type III secretion system (T3SS) is a virulence apparatus existing in many bacterial pathogens. Structurally, T3SS consists of the base, needle, tip, and translocon. The NLRC4 inflammasome is the major receptor for T3SS needle and basal rod proteins. Whether other T3SS components are recognized by NLRC4 is unclear. In this study, using as a model intracellular pathogen, we examined T3SS-inflammasome interaction and its effect on cell death. induced pyroptosis in a manner that required the bacterial translocon and the host inflammasome proteins of NLRC4, NLRP3, ASC, and caspase 1/4. The translocon protein EseB triggered NLRC4/NAIP-mediated pyroptosis by binding NAIP via its C-terminal region, particularly the terminal 6 residues (T6R). EseB homologs exist widely in T3SS-positive bacteria and share high identities in T6R. Like EseB, all of the representatives of the EseB homologs exhibited T6R-dependent NLRC4 activation ability. Together these results revealed the function and molecular mechanism of EseB to induce host cell pyroptosis and suggested a highly conserved inflammasome-activation mechanism of T3SS translocon in bacterial pathogens. |
| title | T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome. |
| topic | Pyroptosis Inflammasomes Type III Secretion Systems Calcium-Binding Proteins CARD Signaling Adaptor Proteins Neuronal Apoptosis-Inhibitory Protein Humans Edwardsiella tarda Apoptosis Regulatory Proteins Animals Bacterial Proteins Mice Host-Pathogen Interactions |
| url | https://pubmed.ncbi.nlm.nih.gov/39951384/ |