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Lookup NU author(s): Dr Giusy MarianoORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Incorporation of disulfide bonds into proteins can be critical for function or stability. In bacterial cells, the periplasmic enzyme DsbA is responsible for disulfide incorporation into many extra-cytoplasmic proteins. The type VI secretion system (T6SS) is a widely occurring nanomachine that delivers toxic effector proteins directly into rival bacterial cells, playing a key role in inter-bacterial competition. We report that two redundant DsbA proteins are required for virulence and for proper deployment of the T6SS in the opportunistic pathogen Serratia marcescens, with several T6SS components being subject to the action of DsbA in secreting cells. Importantly, we demonstrate that DsbA also plays a critical role in recipient target cells, being required for the toxicity of certain incoming effector proteins. Thus we reveal that target cell functions can be hijacked by T6SS effectors for effector activation, adding a further level of complexity to the T6SS-mediated inter-bacterial interactions which define varied microbial communities.
Author(s): Mariano G, Monlezun L, Coulthurst SJ
Publication type: Article
Publication status: Published
Journal: Cell Reports
Print publication date: 16/01/2018
Online publication date: 29/01/2018
Acceptance date: 21/12/2017
Date deposited: 25/08/2020
ISSN (electronic): 2211-1247
Publisher: Cell Press
PubMed id: 29346773
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