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The VgrG Proteins Are “à la Carte” Delivery Systems for Bacterial Type VI Effectors
Open accessAbstract
The bacterial type VI secretion system (T6SS) is a supra-molecular complex akin to bacteriophage tails, with VgrG proteins acting as a puncturing device. The Pseudomonas aeruginosa H1-T6SS has been extensively characterized. It is involved in bacterial killing and in the delivery of three toxins, Tse1-3. Here, we demonstrate the independent contribution of the three H1-T6SS co-regulated vgrG genes, vgrG1abc, to bacterial killing. A putative toxin is encoded in the vicinity of each vgrG gene, supporting the concept of specific VgrG/toxin couples. In this respect, VgrG1c is involved in the delivery of an Rhs protein, RhsP1. The RhsP1 C terminus carries a toxic activity, from which the producing bacterium is protected by a cognate immunity. Similarly, VgrG1a-dependent toxicity is associated with the PA0093 gene encoding a two-domain protein with a putative toxin domain (Toxin_61) at the C terminus. Finally, VgrG1b-dependent killing is detectable upon complementation of a triple vgrG1abc mutant. The VgrG1b-dependent killing is mediated by PA0099, which presents the characteristics of the superfamily nuclease 2 toxin members. Overall, these data develop the concept that VgrGs are indispensable components for the specific delivery of effectors. Several additional vgrG genes are encoded on the P. aeruginosa genome and are not linked genetically to other T6SS genes. A closer inspection of these clusters reveals that they also encode putative toxins. Overall, these associations further support the notion of an original form of secretion system, in which VgrG acts as the carrier.
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Citations
Cited by
The Type VI secretion system: a versatile bacterial weapon
Coulthurst, S. (2019) · Microbiology · doi:10.1099/mic.0.000789 · Cited by 346
Whitney, J. C., Quentin, D., Sawai, S., LeRoux, M., Harding, B. N., Ledvina, H. E., Tran, B. Q., Robinson, H., Goo, Y. A., Goodlett, D. R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.09.027 · Cited by 263
Si, M., Zhao, C., Burkinshaw, B., Zhang, B., Wei, D., Wang, Y., Dong, T. G., & Shen, X. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614902114 · Cited by 245
Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases
Hespanhol, J. T., Sanchez-Limache, D. E., Nicastro, G. G., Mead, L., Llontop, E. E., Chagas-Santos, G., Farah, C. S., de Souza, R. F., Galhardo, R. D. S., Lovering, A. L., et al. (2022) · eLife · doi:10.7554/elife.82437 · Cited by 45
The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors
Kanarek, K., Fridman, C. M., Bosis, E., & Salomon, D. (2023) · Nature Communications · doi:10.1038/s41467-023-40659-2 · Cited by 27
Metadata
- Authors
- Hachani, A., Allsopp, L. P., Oduko, Y., & Filloux, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 289
- Issue
- 25
- Pages
- 17872-17884
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2019374914
- Cited by
- 204
- References
- 0
- FWCI
- 10.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hachani, A., Allsopp, L. P., Oduko, Y., & Filloux, A. (2014). The VgrG Proteins Are “à la Carte” Delivery Systems for Bacterial Type VI Effectors. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m114.563429
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