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The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii

BACKGROUND: Acinetobacter baumannii is an important opportunistic pathogen responsible for various nosocomial infections. The BfmRS two-component system plays a role in pathogenesis and antimicrobial resistance of A. baumannii via regulation of bacterial envelope structures. This study investigated...

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Autores principales: Kim, Se Yeon, Kim, Mi Hyun, Kim, Seung Il, Son, Joo Hee, Kim, Shukho, Lee, Yoo Chul, Shin, Minsang, Oh, Man Hwan, Lee, Je Chul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925498/
https://www.ncbi.nlm.nih.gov/pubmed/31864291
http://dx.doi.org/10.1186/s12866-019-1679-0
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author Kim, Se Yeon
Kim, Mi Hyun
Kim, Seung Il
Son, Joo Hee
Kim, Shukho
Lee, Yoo Chul
Shin, Minsang
Oh, Man Hwan
Lee, Je Chul
author_facet Kim, Se Yeon
Kim, Mi Hyun
Kim, Seung Il
Son, Joo Hee
Kim, Shukho
Lee, Yoo Chul
Shin, Minsang
Oh, Man Hwan
Lee, Je Chul
author_sort Kim, Se Yeon
collection PubMed
description BACKGROUND: Acinetobacter baumannii is an important opportunistic pathogen responsible for various nosocomial infections. The BfmRS two-component system plays a role in pathogenesis and antimicrobial resistance of A. baumannii via regulation of bacterial envelope structures. This study investigated the role of the sensor kinase, BfmS, in localization of outer membrane protein A (OmpA) in the outer membrane and production of outer membrane vesicles (OMVs) using wild-type A. baumannii ATCC 17978, ΔbfmS mutant, and bfmS-complemented strains. RESULTS: The ΔbfmS mutant showed hypermucoid phenotype in the culture plates, growth retardation under static culture conditions, and reduced susceptibility to aztreonam and colistin compared to the wild-type strain. The ΔbfmS mutant produced less OmpA in the outer membrane but released more OmpA via OMVs than the wild-type strain, even though expression of ompA and its protein production were not different between the two strains. The ΔbfmS mutant produced 2.35 times more OMV particles and 4.46 times more OMV proteins than the wild-type stain. The ΔbfmS mutant OMVs were more cytotoxic towards A549 cells than wild-type strain OMVs. CONCLUSIONS: The present study demonstrates that BfmS controls production of OMVs in A. baumannii. Moreover, BfmS negatively regulates antimicrobial resistance of A. baumannii and OMV-mediated host cell cytotoxicity. Our results indicate that BfmS negatively controls the pathogenic traits of A. baumannii via cell envelope structures and OMV production.
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spelling pubmed-69254982019-12-30 The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii Kim, Se Yeon Kim, Mi Hyun Kim, Seung Il Son, Joo Hee Kim, Shukho Lee, Yoo Chul Shin, Minsang Oh, Man Hwan Lee, Je Chul BMC Microbiol Research Article BACKGROUND: Acinetobacter baumannii is an important opportunistic pathogen responsible for various nosocomial infections. The BfmRS two-component system plays a role in pathogenesis and antimicrobial resistance of A. baumannii via regulation of bacterial envelope structures. This study investigated the role of the sensor kinase, BfmS, in localization of outer membrane protein A (OmpA) in the outer membrane and production of outer membrane vesicles (OMVs) using wild-type A. baumannii ATCC 17978, ΔbfmS mutant, and bfmS-complemented strains. RESULTS: The ΔbfmS mutant showed hypermucoid phenotype in the culture plates, growth retardation under static culture conditions, and reduced susceptibility to aztreonam and colistin compared to the wild-type strain. The ΔbfmS mutant produced less OmpA in the outer membrane but released more OmpA via OMVs than the wild-type strain, even though expression of ompA and its protein production were not different between the two strains. The ΔbfmS mutant produced 2.35 times more OMV particles and 4.46 times more OMV proteins than the wild-type stain. The ΔbfmS mutant OMVs were more cytotoxic towards A549 cells than wild-type strain OMVs. CONCLUSIONS: The present study demonstrates that BfmS controls production of OMVs in A. baumannii. Moreover, BfmS negatively regulates antimicrobial resistance of A. baumannii and OMV-mediated host cell cytotoxicity. Our results indicate that BfmS negatively controls the pathogenic traits of A. baumannii via cell envelope structures and OMV production. BioMed Central 2019-12-21 /pmc/articles/PMC6925498/ /pubmed/31864291 http://dx.doi.org/10.1186/s12866-019-1679-0 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Kim, Se Yeon
Kim, Mi Hyun
Kim, Seung Il
Son, Joo Hee
Kim, Shukho
Lee, Yoo Chul
Shin, Minsang
Oh, Man Hwan
Lee, Je Chul
The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title_full The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title_fullStr The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title_full_unstemmed The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title_short The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii
title_sort sensor kinase bfms controls production of outer membrane vesicles in acinetobacter baumannii
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925498/
https://www.ncbi.nlm.nih.gov/pubmed/31864291
http://dx.doi.org/10.1186/s12866-019-1679-0
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