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Peptidylarginine Deiminase Inhibitors Reduce Bacterial Membrane Vesicle Release and Sensitise 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 , 11.06.2019.

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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 Sensitise Bacteria to Antibiotic Treatment. In: Frontiers Cellular and Infection Microbiology . 2019.

Bibtex

@article{41fd3111969c40d089c7d61fcfdc3f76,
title = "Peptidylarginine Deiminase Inhibitors Reduce Bacterial Membrane Vesicle Release and Sensitise 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 catalyse 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 both28 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.",
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 = "11",
language = "English",
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 Sensitise 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 - 2019/6/11

Y1 - 2019/6/11

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 catalyse 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 both28 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 catalyse 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 both28 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.

M3 - Article

JO - Frontiers Cellular and Infection Microbiology

T2 - Frontiers Cellular and Infection Microbiology

JF - Frontiers Cellular and Infection Microbiology

SN - 2235-2988

ER -