A family of Type VI secretion system effector proteins that form ion-selective pores

Giuseppina Mariano, Katharina Trunk, David J. Williams, Laura Monlezun, Henrik Strahl, Samantha J. Pitt, Sarah Coulthurst (Lead / Corresponding author)

Research output: Contribution to journalArticle

1 Citation (Scopus)
32 Downloads (Pure)

Abstract

Type VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.

Original languageEnglish
Article number5484
Pages (from-to)1-15
Number of pages15
JournalNature Communications
Volume10
Issue number1
DOIs
Publication statusPublished - 2 Dec 2019

Fingerprint

effectors
secretions
Genes
Ions
proteins
Membranes
porosity
Bacterial Genomes
Serratia marcescens
Gene encoding
Poisons
Depolarization
Pathogens
Enterobacteriaceae
Cations
Permeability
Bacteria
ions
Proteins
genes

Cite this

@article{05659a46dbf04d01825260206249c2b2,
title = "A family of Type VI secretion system effector proteins that form ion-selective pores",
abstract = "Type VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.",
author = "Giuseppina Mariano and Katharina Trunk and Williams, {David J.} and Laura Monlezun and Henrik Strahl and Pitt, {Samantha J.} and Sarah Coulthurst",
note = "This work was supported by the Wellcome Trust (104556/Z/14/Z, Senior Fellowship in Basic Biomedical Science to S.J.C.; 097818/Z/11/B and 109118/Z/15/Z, PhD studentships to University of Dundee), the MRC (MR/K000111X/1, New Investigator Research Grant to S.J.C.) and the Royal Society of Edinburgh (Biomedical Personal Research Fellowship to S.J.P.). We thank Roland Freudl for the gift of anti-OmpA antibody; Adam Ostrowski for construction of strains AO07 and AO08; Gal Horesh, Amy Dorward and Gavin Robertson for expert assistance; the Flow Cytometry and Cell Sorting Facility at the University of Dundee; and the Dundee Imaging Facility (supported by Wellcome Trust [097945/B/11/Z] and MRC [MR/K015869/1]) awards).",
year = "2019",
month = "12",
day = "2",
doi = "10.1038/s41467-019-13439-0",
language = "English",
volume = "10",
pages = "1--15",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

A family of Type VI secretion system effector proteins that form ion-selective pores. / Mariano, Giuseppina; Trunk, Katharina; Williams, David J.; Monlezun, Laura; Strahl, Henrik; Pitt, Samantha J. ; Coulthurst, Sarah (Lead / Corresponding author).

In: Nature Communications, Vol. 10, No. 1, 5484, 02.12.2019, p. 1-15.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A family of Type VI secretion system effector proteins that form ion-selective pores

AU - Mariano, Giuseppina

AU - Trunk, Katharina

AU - Williams, David J.

AU - Monlezun, Laura

AU - Strahl, Henrik

AU - Pitt, Samantha J.

AU - Coulthurst, Sarah

N1 - This work was supported by the Wellcome Trust (104556/Z/14/Z, Senior Fellowship in Basic Biomedical Science to S.J.C.; 097818/Z/11/B and 109118/Z/15/Z, PhD studentships to University of Dundee), the MRC (MR/K000111X/1, New Investigator Research Grant to S.J.C.) and the Royal Society of Edinburgh (Biomedical Personal Research Fellowship to S.J.P.). We thank Roland Freudl for the gift of anti-OmpA antibody; Adam Ostrowski for construction of strains AO07 and AO08; Gal Horesh, Amy Dorward and Gavin Robertson for expert assistance; the Flow Cytometry and Cell Sorting Facility at the University of Dundee; and the Dundee Imaging Facility (supported by Wellcome Trust [097945/B/11/Z] and MRC [MR/K015869/1]) awards).

PY - 2019/12/2

Y1 - 2019/12/2

N2 - Type VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.

AB - Type VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.

UR - http://www.scopus.com/inward/record.url?scp=85075953240&partnerID=8YFLogxK

U2 - 10.1038/s41467-019-13439-0

DO - 10.1038/s41467-019-13439-0

M3 - Article

C2 - 31792213

VL - 10

SP - 1

EP - 15

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 5484

ER -