nagZ Triggers Gonococcal Biofilm Disassembly

Bacterial-bacterial interactions play a critical role in promoting biofilm formation. Here we show that NagZ, a protein associated with peptidoglycan recycling, has moonlighting activity that allows it to modulate biofilm accumulation by Neisseria gonorrhoeae. We characterize the biochemical propert...

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Main Authors: Bhoopalan, Senthil V., Piekarowicz, Andrzej, Lenz, Jonathan D., Dillard, Joseph P., Stein, Daniel C.
Format: Online
Language:English
Published: Nature Publishing Group 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4772129/
id pubmed-4772129
recordtype oai_dc
spelling pubmed-47721292016-03-07 nagZ Triggers Gonococcal Biofilm Disassembly Bhoopalan, Senthil V. Piekarowicz, Andrzej Lenz, Jonathan D. Dillard, Joseph P. Stein, Daniel C. Article Bacterial-bacterial interactions play a critical role in promoting biofilm formation. Here we show that NagZ, a protein associated with peptidoglycan recycling, has moonlighting activity that allows it to modulate biofilm accumulation by Neisseria gonorrhoeae. We characterize the biochemical properties of NagZ and demonstrate its ability to function as a dispersing agent for biofilms formed on abiotic surfaces. We extend these observations to cell culture and tissue explant models and show that in nagZ mutants, the biofilms formed in cell culture and on human tissues contain significantly more biomass than those formed by a wild-type strain. Our results demonstrate that an enzyme thought to be restricted to peptidoglycan recycling is able to disperse preformed biofilms. Nature Publishing Group 2016-03-01 /pmc/articles/PMC4772129/ /pubmed/26927542 http://dx.doi.org/10.1038/srep22372 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Bhoopalan, Senthil V.
Piekarowicz, Andrzej
Lenz, Jonathan D.
Dillard, Joseph P.
Stein, Daniel C.
spellingShingle Bhoopalan, Senthil V.
Piekarowicz, Andrzej
Lenz, Jonathan D.
Dillard, Joseph P.
Stein, Daniel C.
nagZ Triggers Gonococcal Biofilm Disassembly
author_facet Bhoopalan, Senthil V.
Piekarowicz, Andrzej
Lenz, Jonathan D.
Dillard, Joseph P.
Stein, Daniel C.
author_sort Bhoopalan, Senthil V.
title nagZ Triggers Gonococcal Biofilm Disassembly
title_short nagZ Triggers Gonococcal Biofilm Disassembly
title_full nagZ Triggers Gonococcal Biofilm Disassembly
title_fullStr nagZ Triggers Gonococcal Biofilm Disassembly
title_full_unstemmed nagZ Triggers Gonococcal Biofilm Disassembly
title_sort nagz triggers gonococcal biofilm disassembly
description Bacterial-bacterial interactions play a critical role in promoting biofilm formation. Here we show that NagZ, a protein associated with peptidoglycan recycling, has moonlighting activity that allows it to modulate biofilm accumulation by Neisseria gonorrhoeae. We characterize the biochemical properties of NagZ and demonstrate its ability to function as a dispersing agent for biofilms formed on abiotic surfaces. We extend these observations to cell culture and tissue explant models and show that in nagZ mutants, the biofilms formed in cell culture and on human tissues contain significantly more biomass than those formed by a wild-type strain. Our results demonstrate that an enzyme thought to be restricted to peptidoglycan recycling is able to disperse preformed biofilms.
publisher Nature Publishing Group
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4772129/
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