An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin

Abstract We investigated the colistin resistance mechanism in an Escherichia coli strain (LC711/14) isolated in Italy in 2014, from an urinary tract infection, which was previously shown to express a colistin resistance mechanism different from mcr-1. LC711/14 was found to carry a novel mutation in...

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Autores principales: Antonio Cannatelli, Tommaso Giani, Noemi Aiezza, Vincenzo Di Pilato, Luigi Principe, Francesco Luzzaro, Cesira L. Galeotti, Gian Maria Rossolini
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Publicado: Nature Portfolio 2017
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spelling oai:doaj.org-article:05682e824bff4f1c9b11642ac630e6ec2021-12-02T11:53:03ZAn allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin10.1038/s41598-017-05167-62045-2322https://doaj.org/article/05682e824bff4f1c9b11642ac630e6ec2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05167-6https://doaj.org/toc/2045-2322Abstract We investigated the colistin resistance mechanism in an Escherichia coli strain (LC711/14) isolated in Italy in 2014, from an urinary tract infection, which was previously shown to express a colistin resistance mechanism different from mcr-1. LC711/14 was found to carry a novel mutation in the pmrB gene, resulting in a leucine to proline amino acid substitution at position 10 of the PmrB sensor kinase component of the PmrAB signal transduction system. The role of this substitution in colistin resistance was documented by expression of the wild-type and mutated alleles in a pmrB deletion derivative of the E. coli reference strain MG1655, in which expression of the mutated allele conferred colistin resistance and upregulation of the endogenous pmrHFIJKLM lipid A modification system. Complementation of LC711/14 with the wild-type pmrB allele restored colistin susceptibility and decreased expression of pmrHFIJKLM, confirming the role of this PmrB mutation. Substitution of leucine at position 10 of PmrB with other amino acids (glycine and glutamine) resulted in loss of function, underscoring a key role of this residue which is located in the cytoplasmic secretion domain of the protein. This work demonstrated that mutation in this domain of the PmrB sensor kinase can be responsible for acquired colistin resistance in E. coli strains of clinical origin.Antonio CannatelliTommaso GianiNoemi AiezzaVincenzo Di PilatoLuigi PrincipeFrancesco LuzzaroCesira L. GaleottiGian Maria RossoliniNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-6 (2017)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Antonio Cannatelli
Tommaso Giani
Noemi Aiezza
Vincenzo Di Pilato
Luigi Principe
Francesco Luzzaro
Cesira L. Galeotti
Gian Maria Rossolini
An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
description Abstract We investigated the colistin resistance mechanism in an Escherichia coli strain (LC711/14) isolated in Italy in 2014, from an urinary tract infection, which was previously shown to express a colistin resistance mechanism different from mcr-1. LC711/14 was found to carry a novel mutation in the pmrB gene, resulting in a leucine to proline amino acid substitution at position 10 of the PmrB sensor kinase component of the PmrAB signal transduction system. The role of this substitution in colistin resistance was documented by expression of the wild-type and mutated alleles in a pmrB deletion derivative of the E. coli reference strain MG1655, in which expression of the mutated allele conferred colistin resistance and upregulation of the endogenous pmrHFIJKLM lipid A modification system. Complementation of LC711/14 with the wild-type pmrB allele restored colistin susceptibility and decreased expression of pmrHFIJKLM, confirming the role of this PmrB mutation. Substitution of leucine at position 10 of PmrB with other amino acids (glycine and glutamine) resulted in loss of function, underscoring a key role of this residue which is located in the cytoplasmic secretion domain of the protein. This work demonstrated that mutation in this domain of the PmrB sensor kinase can be responsible for acquired colistin resistance in E. coli strains of clinical origin.
format article
author Antonio Cannatelli
Tommaso Giani
Noemi Aiezza
Vincenzo Di Pilato
Luigi Principe
Francesco Luzzaro
Cesira L. Galeotti
Gian Maria Rossolini
author_facet Antonio Cannatelli
Tommaso Giani
Noemi Aiezza
Vincenzo Di Pilato
Luigi Principe
Francesco Luzzaro
Cesira L. Galeotti
Gian Maria Rossolini
author_sort Antonio Cannatelli
title An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
title_short An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
title_full An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
title_fullStr An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
title_full_unstemmed An allelic variant of the PmrB sensor kinase responsible for colistin resistance in an Escherichia coli strain of clinical origin
title_sort allelic variant of the pmrb sensor kinase responsible for colistin resistance in an escherichia coli strain of clinical origin
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/05682e824bff4f1c9b11642ac630e6ec
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