Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis
Abstract Lawsonia intracellularis, the etiologic agent of proliferative enteropathy (PE), is an obligate intracellular Gram-negative bacterium possessing a type III secretion system (T3SS), which enables the pathogen to translocate effector proteins into targeted host cells to modulate their functio...
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| Format: | Article |
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BMC
2023-11-01
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| Series: | Veterinary Research |
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| Online Access: | https://doi.org/10.1186/s13567-023-01243-0 |
| _version_ | 1827633431944626176 |
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| author | Beibei Huang Zihe Zhu Yimin Dai Chengxian Yan Jingyu Xu Lingling Sun Qinghua Zhang Xuejiao An Fenju Lai |
| author_facet | Beibei Huang Zihe Zhu Yimin Dai Chengxian Yan Jingyu Xu Lingling Sun Qinghua Zhang Xuejiao An Fenju Lai |
| author_sort | Beibei Huang |
| collection | DOAJ |
| description | Abstract Lawsonia intracellularis, the etiologic agent of proliferative enteropathy (PE), is an obligate intracellular Gram-negative bacterium possessing a type III secretion system (T3SS), which enables the pathogen to translocate effector proteins into targeted host cells to modulate their functions. T3SS is a syringe-like apparatus consisting of a base, an extracellular needle, a tip, and a translocon. The translocon proteins assembled by two hydrophobic membrane proteins can form pores in the host-cell membrane, and therefore play an essential role in the function of T3SS. To date, little is known about the T3SS and translocon proteins of L. intracellularis. In this study, we first analyzed the conservation of the T3S apparatus between L. intracellularis and Yersinia, and characterized the putative T3S hydrophobic major translocon protein LI1158 and minor translocon protein LI1159 in the L. intracellularis genome. Then, by using Yersinia pseudotuberculosis as a surrogate system, we found that the full-length LI1158 and LI1159 proteins, but not the putative class II chaperone LI1157, were secreted in a − Ca2+ and T3SS-dependent manner and the secretion signal was located at the N terminus (aa 1–40). Furthermore, yeast-two hybrid experiments revealed that LI1158 and LI1159 could self-interact, and LI1159 could interact with LI1157. However, unlike CPn0809 and YopB, which are the major hydrophobic translocon proteins of the T3SS of C. pneumoniae and Yersinia, respectively, full-length LI1158 was non-toxic to both yeast and Escherichia coli cells, but full-length LI1159 showed certain toxicity to E. coli cells. Taken together, despite some differences from the findings in other bacteria, our results demonstrate that LI1158 and LI1159 may be the translocon proteins of L. intracellularis T3SS, and probably play important roles in the translocation of effector proteins at the early pathogen infection stage. |
| first_indexed | 2024-03-09T14:59:01Z |
| format | Article |
| id | doaj.art-610e0d8b03dc4e559cdc2076afc44150 |
| institution | Directory Open Access Journal |
| issn | 1297-9716 |
| language | English |
| last_indexed | 2024-03-09T14:59:01Z |
| publishDate | 2023-11-01 |
| publisher | BMC |
| record_format | Article |
| series | Veterinary Research |
| spelling | doaj.art-610e0d8b03dc4e559cdc2076afc441502023-11-26T13:59:54ZengBMCVeterinary Research1297-97162023-11-0154111510.1186/s13567-023-01243-0Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularisBeibei Huang0Zihe Zhu1Yimin Dai2Chengxian Yan3Jingyu Xu4Lingling Sun5Qinghua Zhang6Xuejiao An7Fenju Lai8School of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Animal Science and Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversitySchool of Bioscience and Bioengineering, Nanchang Key Laboratory of Fermentation Application Technology, Jiangxi Agricultural UniversityJiangxi Engineering Laboratory for the Development and Utilization of Agricultural Microbial ResourcesAbstract Lawsonia intracellularis, the etiologic agent of proliferative enteropathy (PE), is an obligate intracellular Gram-negative bacterium possessing a type III secretion system (T3SS), which enables the pathogen to translocate effector proteins into targeted host cells to modulate their functions. T3SS is a syringe-like apparatus consisting of a base, an extracellular needle, a tip, and a translocon. The translocon proteins assembled by two hydrophobic membrane proteins can form pores in the host-cell membrane, and therefore play an essential role in the function of T3SS. To date, little is known about the T3SS and translocon proteins of L. intracellularis. In this study, we first analyzed the conservation of the T3S apparatus between L. intracellularis and Yersinia, and characterized the putative T3S hydrophobic major translocon protein LI1158 and minor translocon protein LI1159 in the L. intracellularis genome. Then, by using Yersinia pseudotuberculosis as a surrogate system, we found that the full-length LI1158 and LI1159 proteins, but not the putative class II chaperone LI1157, were secreted in a − Ca2+ and T3SS-dependent manner and the secretion signal was located at the N terminus (aa 1–40). Furthermore, yeast-two hybrid experiments revealed that LI1158 and LI1159 could self-interact, and LI1159 could interact with LI1157. However, unlike CPn0809 and YopB, which are the major hydrophobic translocon proteins of the T3SS of C. pneumoniae and Yersinia, respectively, full-length LI1158 was non-toxic to both yeast and Escherichia coli cells, but full-length LI1159 showed certain toxicity to E. coli cells. Taken together, despite some differences from the findings in other bacteria, our results demonstrate that LI1158 and LI1159 may be the translocon proteins of L. intracellularis T3SS, and probably play important roles in the translocation of effector proteins at the early pathogen infection stage.https://doi.org/10.1186/s13567-023-01243-0Proliferative enteropathyLawsonia intracellularistype III secretion systemtranslocon proteins |
| spellingShingle | Beibei Huang Zihe Zhu Yimin Dai Chengxian Yan Jingyu Xu Lingling Sun Qinghua Zhang Xuejiao An Fenju Lai Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis Veterinary Research Proliferative enteropathy Lawsonia intracellularis type III secretion system translocon proteins |
| title | Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis |
| title_full | Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis |
| title_fullStr | Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis |
| title_full_unstemmed | Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis |
| title_short | Characterization of translocon proteins in the type III secretion system of Lawsonia intracellularis |
| title_sort | characterization of translocon proteins in the type iii secretion system of lawsonia intracellularis |
| topic | Proliferative enteropathy Lawsonia intracellularis type III secretion system translocon proteins |
| url | https://doi.org/10.1186/s13567-023-01243-0 |
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