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The Pseudomonas aeruginosa T6SS Delivers a Periplasmic Toxin that Disrupts Bacterial Cell Morphology.

Published version
Peer-reviewed

Type

Article

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Authors

Wood, Thomas E 
Howard, Sophie A 
Förster, Andreas 
Nolan, Laura M 
Manoli, Eleni 

Abstract

The type VI secretion system (T6SS) is crucial in interbacterial competition and is a virulence determinant of many Gram-negative bacteria. Several T6SS effectors are covalently fused to secreted T6SS structural components such as the VgrG spike for delivery into target cells. In Pseudomonas aeruginosa, the VgrG2b effector was previously proposed to mediate bacterial internalization into eukaryotic cells. In this work, we find that the VgrG2b C-terminal domain (VgrG2bC-ter) elicits toxicity in the bacterial periplasm, counteracted by a cognate immunity protein. We resolve the structure of VgrG2bC-ter and confirm it is a member of the zinc-metallopeptidase family of enzymes. We show that this effector causes membrane blebbing at midcell, which suggests a distinct type of T6SS-mediated growth inhibition through interference with cell division, mimicking the impact of β-lactam antibiotics. Our study introduces a further effector family to the T6SS arsenal and demonstrates that VgrG2b can target both prokaryotic and eukaryotic cells.

Description

Keywords

Pseudomonas aeruginosa, VgrG, effector, metallopeptidase, type VI secretion system, Anti-Bacterial Agents, Bacterial Proteins, Bacterial Secretion Systems, Periplasm, Pseudomonas aeruginosa, Type VI Secretion Systems, Virulence Factors, beta-Lactams

Journal Title

Cell Rep

Conference Name

Journal ISSN

2211-1247
2211-1247

Volume Title

29

Publisher

Elsevier BV
Sponsorship
Medical Research Council (MR/N000846/1)