University of Hertfordshire

From the same journal

By the same authors

Standard

Peptidylarginine deiminase inhibitors reduce bacterial membrane vesicle release and sensitize bacteria to antibiotic treatment. / Kosgodage, Uchini S; Matewele, Paul; Mastroianni, Giulia; Lange, Sigrun; Kraev, Igor; Brotherton, Dominik; Awamaria, Brigitte; Nicholas, Anthony P.; Inal, Jameel.

In: Frontiers Cellular and Infection Microbiology , Vol. 9, 227, 27.06.2019.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Kosgodage, Uchini S ; Matewele, Paul ; Mastroianni, Giulia ; Lange, Sigrun ; Kraev, Igor ; Brotherton, Dominik ; Awamaria, Brigitte ; Nicholas, Anthony P. ; Inal, Jameel. / Peptidylarginine deiminase inhibitors reduce bacterial membrane vesicle release and sensitize bacteria to antibiotic treatment. In: Frontiers Cellular and Infection Microbiology . 2019 ; Vol. 9.

Bibtex

@article{41fd3111969c40d089c7d61fcfdc3f76,
title = "Peptidylarginine deiminase inhibitors reduce bacterial membrane vesicle release and sensitize bacteria to antibiotic treatment",
abstract = "Outer membrane and membrane vesicles (OMV/MV) are released from bacteria and participate in cell communication, biofilm formation and host-pathogen interactions. Peptidylarginine deiminases (PADs) are phylogenetically conserved enzymes that catalyze post-translational deimination/citrullination of proteins, causing structural and functional changes in target proteins. PADs also play major roles in the regulation of eukaryotic extracellular vesicle release. Here we show phylogenetically conserved pathways of PAD-mediated OMV/MV release in bacteria and describe deiminated/citrullinated proteins in E. coli and their derived OMV/MVs. Furthermore, we show that PAD inhibitors can be used to effectively reduce OMV/MV release, both in Gram-negative and Gram-positive bacteria. Importantly, this resulted in enhanced antibiotic sensitivity of both E. coli and S. aureus to a range of antibiotics tested. Our findings reveal novel strategies for applying pharmacological OMV/MV-inhibition to reduce antibiotic resistance.",
keywords = "Antibiotic sensitivity, Deimination/citrullination, E. coli VCS257, Outer-membrane vesicles (OMVs), Peptidylarginine deiminase (PAD), S. aureus subsp. aureus Rosenbach",
author = "Kosgodage, {Uchini S} and Paul Matewele and Giulia Mastroianni and Sigrun Lange and Igor Kraev and Dominik Brotherton and Brigitte Awamaria and Nicholas, {Anthony P.} and Jameel Inal",
year = "2019",
month = "6",
day = "27",
doi = "10.3389/fcimb.2019.00227",
language = "English",
volume = "9",
journal = "Frontiers Cellular and Infection Microbiology",
issn = "2235-2988",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Peptidylarginine deiminase inhibitors reduce bacterial membrane vesicle release and sensitize bacteria to antibiotic treatment

AU - Kosgodage, Uchini S

AU - Matewele, Paul

AU - Mastroianni, Giulia

AU - Lange, Sigrun

AU - Kraev, Igor

AU - Brotherton, Dominik

AU - Awamaria, Brigitte

AU - Nicholas, Anthony P.

AU - Inal, Jameel

PY - 2019/6/27

Y1 - 2019/6/27

N2 - Outer membrane and membrane vesicles (OMV/MV) are released from bacteria and participate in cell communication, biofilm formation and host-pathogen interactions. Peptidylarginine deiminases (PADs) are phylogenetically conserved enzymes that catalyze post-translational deimination/citrullination of proteins, causing structural and functional changes in target proteins. PADs also play major roles in the regulation of eukaryotic extracellular vesicle release. Here we show phylogenetically conserved pathways of PAD-mediated OMV/MV release in bacteria and describe deiminated/citrullinated proteins in E. coli and their derived OMV/MVs. Furthermore, we show that PAD inhibitors can be used to effectively reduce OMV/MV release, both in Gram-negative and Gram-positive bacteria. Importantly, this resulted in enhanced antibiotic sensitivity of both E. coli and S. aureus to a range of antibiotics tested. Our findings reveal novel strategies for applying pharmacological OMV/MV-inhibition to reduce antibiotic resistance.

AB - Outer membrane and membrane vesicles (OMV/MV) are released from bacteria and participate in cell communication, biofilm formation and host-pathogen interactions. Peptidylarginine deiminases (PADs) are phylogenetically conserved enzymes that catalyze post-translational deimination/citrullination of proteins, causing structural and functional changes in target proteins. PADs also play major roles in the regulation of eukaryotic extracellular vesicle release. Here we show phylogenetically conserved pathways of PAD-mediated OMV/MV release in bacteria and describe deiminated/citrullinated proteins in E. coli and their derived OMV/MVs. Furthermore, we show that PAD inhibitors can be used to effectively reduce OMV/MV release, both in Gram-negative and Gram-positive bacteria. Importantly, this resulted in enhanced antibiotic sensitivity of both E. coli and S. aureus to a range of antibiotics tested. Our findings reveal novel strategies for applying pharmacological OMV/MV-inhibition to reduce antibiotic resistance.

KW - Antibiotic sensitivity

KW - Deimination/citrullination

KW - E. coli VCS257

KW - Outer-membrane vesicles (OMVs)

KW - Peptidylarginine deiminase (PAD)

KW - S. aureus subsp. aureus Rosenbach

UR - http://www.scopus.com/inward/record.url?scp=85068897821&partnerID=8YFLogxK

U2 - 10.3389/fcimb.2019.00227

DO - 10.3389/fcimb.2019.00227

M3 - Article

VL - 9

JO - Frontiers Cellular and Infection Microbiology

JF - Frontiers Cellular and Infection Microbiology

SN - 2235-2988

M1 - 227

ER -