| Structural highlights
Function
TSE5_PSEAE Toxin secreted by the H1 type VI (H1-T6SS) secretion system that acts on bacterial target cells. The producing bacterium is protected by a cognate immunity protein.[1] [2]
Publication Abstract from PubMed
Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 A cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled with an extensive array of biophysical and genetic investigations, unravels the multifaceted functional mechanisms of Tse5. The data suggest that interfacial Tse5-membrane binding delivers its encapsulated pore-forming toxin fragment to the target bacterial membrane, where it assembles pores that cause cell depolarisation and, ultimately, bacterial death.
Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.,Gonzalez-Magana A, Tascon I, Altuna-Alvarez J, Queralt-Martin M, Colautti J, Velazquez C, Zabala M, Rojas-Palomino J, Cardenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jove D Nat Commun. 2023 Nov 28;14(1):7808. doi: 10.1038/s41467-023-43585-5. PMID:38016939[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Whitney JC, Beck CM, Goo YA, Russell AB, Harding BN, De Leon JA, Cunningham DA, Tran BQ, Low DA, Goodlett DR, Hayes CS, Mougous JD. Genetically distinct pathways guide effector export through the type VI secretion system. Mol Microbiol. 2014 May;92(3):529-42. PMID:24589350 doi:10.1111/mmi.12571
- ↑ Hachani A, Allsopp LP, Oduko Y, Filloux A. The VgrG proteins are "a la carte" delivery systems for bacterial type VI effectors. J Biol Chem. 2014 Jun 20;289(25):17872-84. doi: 10.1074/jbc.M114.563429. Epub , 2014 May 2. PMID:24794869 doi:http://dx.doi.org/10.1074/jbc.M114.563429
- ↑ González-Magaña A, Tascón I, Altuna-Alvarez J, Queralt-Martín M, Colautti J, Velázquez C, Zabala M, Rojas-Palomino J, Cárdenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jové D. Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. Nat Commun. 2023 Nov 28;14(1):7808. PMID:38016939 doi:10.1038/s41467-023-43585-5
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