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Updated: Nov 9, 2025

Replication of the Ordered, Nonredundant Library of Pseudomonas aeruginosa strain PA14 Transposon Insertion Mutants
Published on: May 4, 2018
The Pseudomonas aeruginosa PAAR2 cluster encodes a putative VRR-NUC domain-containing effector
Shuangyue Wang1, Zhi Geng2, Heng Zhang2
1Institutes of Physical Science and Information Technology, Anhui University, Hefei, China.
Abstract:
The bacterial type VI secretion system (T6SS) secretes many toxic effectors to gain advantage in inter-bacterial competition and for eukaryotic host infection. The cognate immunity proteins of these effectors protect bacteria from the virulence of their own effectors. The T6SS injects its inner-needle Hcp tube, the sharpening tip complex -consisting of VgrG and proline-alanine-alanine-arginine repeats (PAAR) proteins- and toxic effectors into neighboring cells. Its functions are largely determined by the activities of its delivered effectors. Five PAAR proteins were found in the Pseudomonas aeruginosa PAO1 genome with three of them shown to facilitate the delivery of various effectors. Here, we report a putative virus-type replication-repair nuclease domain-containing effector TseV encoded by the least investigated P. aeruginosa PAAR2 cluster. The crystal structure of its putative cognate effector TsiV is presented at 1.6 Å resolution. Through structure and sequence comparisons, we propose TseV-TsiV to be a putative novel effector-immunity (E-I) pair and we discuss the roles of other PAAR2 cluster encoded proteins.
Insights
Researchers identified a novel effector-immunity pair, TseV-TsiV, in Pseudomonas aeruginosa. This discovery sheds light on the bacterial type VI secretion system
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Structural Biology
Background:
- The bacterial type VI secretion system (T6SS) is crucial for inter-bacterial competition and host infection, delivering toxic effectors.
- Cognate immunity proteins protect bacteria from self-inflicted effector toxicity.
- Pseudomonas aeruginosa possesses five proline-alanine-alanine-arginine (PAAR) proteins, with some facilitating effector delivery.
Purpose of the Study:
- To investigate a putative novel effector, TseV, containing a virus-type replication-repair nuclease domain, encoded by the P. aeruginosa PAAR2 cluster.
- To determine the crystal structure of the putative cognate immunity protein, TsiV.
- To propose TseV-TsiV as a novel effector-immunity (E-I) pair and explore the functions of other PAAR2 cluster proteins.
Main Methods:
- X-ray crystallography was used to determine the 1.6 Å resolution structure of TsiV.
- Sequence and structural comparisons were employed to analyze the TseV-TsiV interaction.
- Bioinformatic analysis of the PAAR2 cluster and its encoded proteins.
Main Results:
- The crystal structure of the putative immunity protein TsiV was solved at 1.6 Å resolution.
- Structural and sequence analyses suggest that TseV and TsiV form a novel effector-immunity pair.
- The study highlights the under-investigated PAAR2 cluster in P. aeruginosa.
Conclusions:
- The TseV-TsiV system represents a newly identified effector-immunity pair within the P. aeruginosa T6SS.
- This finding expands our understanding of T6SS diversity and function.
- Further research into the PAAR2 cluster may reveal additional mechanisms of bacterial virulence and competition.
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