scholarly journals Acinetobacter baumannii Utilizes a Type VI Secretion System for Bacterial Competition

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e59388 ◽  
Author(s):  
Michael D. Carruthers ◽  
Paul A. Nicholson ◽  
Erin N. Tracy ◽  
Robert S. Munson
2020 ◽  
Vol 11 (1) ◽  
Author(s):  
William P. J. Smith ◽  
Maj Brodmann ◽  
Daniel Unterweger ◽  
Yohan Davit ◽  
Laurie E. Comstock ◽  
...  

Abstract Tit-for-tat is a familiar principle from animal behavior: individuals respond in kind to being helped or harmed by others. Remarkably some bacteria appear to display tit-for-tat behavior, but how this evolved is not understood. Here we combine evolutionary game theory with agent-based modelling of bacterial tit-for-tat, whereby cells stab rivals with poisoned needles (the type VI secretion system) after being stabbed themselves. Our modelling shows tit-for-tat retaliation is a surprisingly poor evolutionary strategy, because tit-for-tat cells lack the first-strike advantage of preemptive attackers. However, if cells retaliate strongly and fire back multiple times, we find that reciprocation is highly effective. We test our predictions by competing Pseudomonas aeruginosa (a tit-for-tat species) with Vibrio cholerae (random-firing), revealing that P. aeruginosa does indeed fire multiple times per incoming attack. Our work suggests bacterial competition has led to a particular form of reciprocation, where the principle is that of strong retaliation, or ‘tits-for-tat’.


2019 ◽  
Vol 8 (7) ◽  
Author(s):  
Helena L. Spiewak ◽  
Sravanthi Shastri ◽  
Lili Zhang ◽  
Stephan Schwager ◽  
Leo Eberl ◽  
...  

2014 ◽  
Vol 70 (4) ◽  
pp. 1094-1103 ◽  
Author(s):  
Xuan Yang ◽  
Min Xu ◽  
Yanying Wang ◽  
Pengyan Xia ◽  
Shuo Wang ◽  
...  

VgrG proteins form the spike of the type VI secretion system (T6SS) syringe-like complex. VgrG3 ofVibrio choleraedegrades the peptidoglycan cell wall of rival bacteriaviaits C-terminal region (VgrG3C) through its muramidase activity. VgrG3C consists of a peptidoglycan-binding domain (VgrG3CPGB) and a putative catalytic domain (VgrG3CCD), and its activity can be inhibited by its immunity protein partner TsiV3. Here, the crystal structure ofV. choleraeVgrG3CCDin complex with TsiV3 is presented at 2.3 Å resolution. VgrG3CCDadopts a chitosanase fold. A dimer of TsiV3 is bound in the deep active-site groove of VgrG3CCD, occluding substrate binding and distorting the conformation of the catalytic dyad. Gln91 and Arg92 of TsiV3 are located in the centre of the interface and are important for recognition of VgrG3C. Mutation of these residues destabilized the complex and abolished the inhibitory activity of TsiV3 against VgrG3C toxicity in cells. Disruption of TsiV3 dimerization also weakened the complex and impaired the inhibitory activity. These structural, biochemical and functional data define the molecular mechanism underlying the self-protection ofV. choleraeand expand the understanding of the role of T6SS in bacterial competition.


PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e89411 ◽  
Author(s):  
Victorien Decoin ◽  
Corinne Barbey ◽  
Dorian Bergeau ◽  
Xavier Latour ◽  
Marc G. J. Feuilloley ◽  
...  

2019 ◽  
Vol 116 (4) ◽  
pp. 1378-1383 ◽  
Author(s):  
Gisela Di Venanzio ◽  
Ki Hwan Moon ◽  
Brent S. Weber ◽  
Juvenal Lopez ◽  
Pek Man Ly ◽  
...  

Acinetobacter baumannii (Ab) is a nosocomial pathogen with one of the highest rates of multidrug resistance (MDR). This is partially due to transmissible plasmids. Many Ab strains harbor a constitutively active type VI secretion system (T6SS) that is employed to kill nonkin bacteria. T6SS and plasmid conjugation both involve cell-to-cell contact. Paradoxically, successful conjugation requires the survival of the recipient, which is the target of the T6SS. Thus, an active T6SS in either the donor or the recipient poses a challenge to plasmid conjugation. Here, we show that large conjugative MDR plasmids heavily rely on their distinctive ability to repress the T6SS of their hosts to enable their own dissemination and the conjugation of other plasmids, contributing to the propagation of MDR among Acinetobacter isolates.


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