Intramolecular chaperone-mediated secretion of an Rhs effector toxin by a type VI secretion system

Tong-Tong Pei, Hao Li, Xiaoye Liang, Zeng-Hang Wang, Guangfeng Liu, Li-Li Wu, Haeun Kim, Zhiping Xie, Ming Yu, Shuangjun Lin, Ping Xu and Tao G. Dong ()
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Tong-Tong Pei: Shanghai Jiao Tong University
Hao Li: Shanghai Jiao Tong University
Xiaoye Liang: Shanghai Jiao Tong University
Zeng-Hang Wang: Shanghai Jiao Tong University
Guangfeng Liu: Chinese Academy of Sciences
Li-Li Wu: Shanghai Jiao Tong University
Haeun Kim: University of Calgary
Zhiping Xie: Shanghai Jiao Tong University
Ming Yu: Shanghai Jiao Tong University
Shuangjun Lin: Shanghai Jiao Tong University
Ping Xu: Shanghai Jiao Tong University
Tao G. Dong: Shanghai Jiao Tong University

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract Bacterial Rhs proteins containing toxic domains are often secreted by type VI secretion systems (T6SSs) through unclear mechanisms. Here, we show that the T6SS Rhs-family effector TseI of Aeromonas dhakensis is subject to self-cleavage at both the N- and the C-terminus, releasing the middle Rhs core and two VgrG-interacting domains (which we name VIRN and VIRC). VIRC is an endonuclease, and the immunity protein TsiI protects against VIRC toxicity through direct interaction. Proteolytic release of VIRC and VIRN is mediated, respectively, by an internal aspartic protease activity and by two conserved glutamic residues in the Rhs core. Mutations abolishing self-cleavage do not block secretion, but reduce TseI toxicity. Deletion of VIRN or the Rhs core abolishes secretion. TseI homologs from Pseudomonas syringae, P. aeruginosa, and Vibrio parahaemolyticus are also self-cleaved. VIRN and VIRC interact with protein VgrG1, while the Rhs core interacts with protein TecI. We propose that VIRN and the Rhs core act as T6SS intramolecular chaperones to facilitate toxin secretion and function.

Date: 2020
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DOI: 10.1038/s41467-020-15774-z

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