A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella
ABSTRACTFlagella play a crucial role in the invasion process of Salmonella and function as a significant antigen that triggers host pyroptosis. Regulation of flagellar biogenesis is essential for both pathogenicity and immune escape of Salmonella. We identified the conserved and unknown function pro...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2024-12-01
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| Series: | Virulence |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/21505594.2024.2331265 |
| _version_ | 1797243077044207616 |
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| author | Yuanji Dai Ruirui Liu Yingying Yue Nannan Song Haihong Jia Zhongrui Ma Xueyan Gao Min Zhang Xilu Yuan Qing Liu Xiaoyu Liu Bingqing Li Weiwei Wang |
| author_facet | Yuanji Dai Ruirui Liu Yingying Yue Nannan Song Haihong Jia Zhongrui Ma Xueyan Gao Min Zhang Xilu Yuan Qing Liu Xiaoyu Liu Bingqing Li Weiwei Wang |
| author_sort | Yuanji Dai |
| collection | DOAJ |
| description | ABSTRACTFlagella play a crucial role in the invasion process of Salmonella and function as a significant antigen that triggers host pyroptosis. Regulation of flagellar biogenesis is essential for both pathogenicity and immune escape of Salmonella. We identified the conserved and unknown function protein STM0435 as a new flagellar regulator. The ∆stm0435 strain exhibited higher pathogenicity in both cellular and animal infection experiments than the wild-type Salmonella. Proteomic and transcriptomic analyses demonstrated dramatic increases in almost all flagellar genes in the ∆stm0435 strain compared to wild-type Salmonella. In a surface plasmon resonance assay, purified STM0435 protein-bound c-di-GMP had an affinity of ~8.383 µM. The crystal structures of apo-STM0435 and STM0435&c-di-GMP complex were determined. Structural analysis revealed that R33, R137, and D138 of STM0435 were essential for c-di-GMP binding. A Salmonella with STM1987 (GGDEF protein) or STM4264 (EAL protein) overexpression exhibits completely different motility behaviours, indicating that the binding of c-di-GMP to STM0435 promotes its inhibitory effect on Salmonella flagellar biogenesis. |
| first_indexed | 2024-04-24T18:49:22Z |
| format | Article |
| id | doaj.art-3a6be38eab514d0c8a02f5b0c26523e7 |
| institution | Directory Open Access Journal |
| issn | 2150-5594 2150-5608 |
| language | English |
| last_indexed | 2024-04-24T18:49:22Z |
| publishDate | 2024-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Virulence |
| spelling | doaj.art-3a6be38eab514d0c8a02f5b0c26523e72024-03-27T04:21:53ZengTaylor & Francis GroupVirulence2150-55942150-56082024-12-0115110.1080/21505594.2024.2331265A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in SalmonellaYuanji Dai0Ruirui Liu1Yingying Yue2Nannan Song3Haihong Jia4Zhongrui Ma5Xueyan Gao6Min Zhang7Xilu Yuan8Qing Liu9Xiaoyu Liu10Bingqing Li11Weiwei Wang12Department of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaMedical Science and Technology Innovation Center, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, Shandong, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, ChinaDepartment of Pathogen Biology, School of Clinical and Basic Medical Sciences, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaDepartment of Clinical Laboratory, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong, ChinaABSTRACTFlagella play a crucial role in the invasion process of Salmonella and function as a significant antigen that triggers host pyroptosis. Regulation of flagellar biogenesis is essential for both pathogenicity and immune escape of Salmonella. We identified the conserved and unknown function protein STM0435 as a new flagellar regulator. The ∆stm0435 strain exhibited higher pathogenicity in both cellular and animal infection experiments than the wild-type Salmonella. Proteomic and transcriptomic analyses demonstrated dramatic increases in almost all flagellar genes in the ∆stm0435 strain compared to wild-type Salmonella. In a surface plasmon resonance assay, purified STM0435 protein-bound c-di-GMP had an affinity of ~8.383 µM. The crystal structures of apo-STM0435 and STM0435&c-di-GMP complex were determined. Structural analysis revealed that R33, R137, and D138 of STM0435 were essential for c-di-GMP binding. A Salmonella with STM1987 (GGDEF protein) or STM4264 (EAL protein) overexpression exhibits completely different motility behaviours, indicating that the binding of c-di-GMP to STM0435 promotes its inhibitory effect on Salmonella flagellar biogenesis.https://www.tandfonline.com/doi/10.1080/21505594.2024.2331265Salmonella typhimuriumc-di-GMPSTM0435flagellar biosynthesisvirulence |
| spellingShingle | Yuanji Dai Ruirui Liu Yingying Yue Nannan Song Haihong Jia Zhongrui Ma Xueyan Gao Min Zhang Xilu Yuan Qing Liu Xiaoyu Liu Bingqing Li Weiwei Wang A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella Virulence Salmonella typhimurium c-di-GMP STM0435 flagellar biosynthesis virulence |
| title | A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella |
| title_full | A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella |
| title_fullStr | A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella |
| title_full_unstemmed | A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella |
| title_short | A c-di-GMP binding effector STM0435 modulates flagellar motility and pathogenicity in Salmonella |
| title_sort | c di gmp binding effector stm0435 modulates flagellar motility and pathogenicity in salmonella |
| topic | Salmonella typhimurium c-di-GMP STM0435 flagellar biosynthesis virulence |
| url | https://www.tandfonline.com/doi/10.1080/21505594.2024.2331265 |
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