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Chimeric Adaptor Proteins Translocate Diverse Type VI Secretion System Effectors in Vibrio Cholerae

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Journal EMBO J
Date 2015 Jul 22
PMID 26194724
Citations 76
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Abstract

Vibrio cholerae is a diverse species of Gram-negative bacteria, commonly found in the aquatic environment and the causative agent of the potentially deadly disease cholera. These bacteria employ a type VI secretion system (T6SS) when they encounter prokaryotic and eukaryotic competitors. This contractile puncturing device translocates a set of effector proteins into neighboring cells. Translocated effectors are toxic unless the targeted cell produces immunity proteins that bind and deactivate incoming effectors. Comparison of multiple V. cholerae strains indicates that effectors are encoded in T6SS effector modules on mobile genetic elements. We identified a diverse group of chimeric T6SS adaptor proteins required for the translocation of diverse effectors encoded in modules. An example for a T6SS effector that requires T6SS adaptor protein 1 (Tap-1) is TseL found in pandemic V. cholerae O1 serogroup strains and other clinical isolates. We propose a model in which Tap-1 is required for loading TseL onto the secretion apparatus. After T6SS-mediated TseL export is completed, Tap-1 is retained in the bacterial cell to load other T6SS machines.

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References
1.
Silverman J, Agnello D, Zheng H, Andrews B, Li M, Catalano C . Haemolysin coregulated protein is an exported receptor and chaperone of type VI secretion substrates. Mol Cell. 2013; 51(5):584-93. PMC: 3844553. DOI: 10.1016/j.molcel.2013.07.025. View

2.
Kelley L, Mezulis S, Yates C, Wass M, Sternberg M . The Phyre2 web portal for protein modeling, prediction and analysis. Nat Protoc. 2015; 10(6):845-58. PMC: 5298202. DOI: 10.1038/nprot.2015.053. View

3.
Unterweger D, Kitaoka M, Miyata S, Bachmann V, Brooks T, Moloney J . Constitutive type VI secretion system expression gives Vibrio cholerae intra- and interspecific competitive advantages. PLoS One. 2012; 7(10):e48320. PMC: 3482179. DOI: 10.1371/journal.pone.0048320. View

4.
Salomon D, Kinch L, Trudgian D, Guo X, Klimko J, Grishin N . Marker for type VI secretion system effectors. Proc Natl Acad Sci U S A. 2014; 111(25):9271-6. PMC: 4078801. DOI: 10.1073/pnas.1406110111. View

5.
Stamatakis A . RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies. Bioinformatics. 2014; 30(9):1312-3. PMC: 3998144. DOI: 10.1093/bioinformatics/btu033. View