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Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force
Swarming contributes to Proteus mirabilis pathogenicity by facilitating access to the catheterized urinary tract. We previously demonstrated that 0.1–20 mmol/L arginine promotes swarming on normally nonpermissive media and that putrescine biosynthesis is required for arginine-induced swarming. We al...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BlackWell Publishing Ltd
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4234256/ https://www.ncbi.nlm.nih.gov/pubmed/25100003 http://dx.doi.org/10.1002/mbo3.194 |
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author | Armbruster, Chelsie E Hodges, Steven A Smith, Sara N Alteri, Christopher J Mobley, Harry L T |
author_facet | Armbruster, Chelsie E Hodges, Steven A Smith, Sara N Alteri, Christopher J Mobley, Harry L T |
author_sort | Armbruster, Chelsie E |
collection | PubMed |
description | Swarming contributes to Proteus mirabilis pathogenicity by facilitating access to the catheterized urinary tract. We previously demonstrated that 0.1–20 mmol/L arginine promotes swarming on normally nonpermissive media and that putrescine biosynthesis is required for arginine-induced swarming. We also previously determined that arginine-induced swarming is pH dependent, indicating that the external proton concentration is critical for arginine-dependent effects on swarming. In this study, we utilized survival at pH 5 and motility as surrogates for measuring changes in the proton gradient (ΔpH) and proton motive force (μH(+)) in response to arginine. We determined that arginine primarily contributes to ΔpH (and therefore μH(+)) through the action of arginine decarboxylase (speA), independent of the role of this enzyme in putrescine biosynthesis. In addition to being required for motility, speA also contributed to fitness during infection. In conclusion, consumption of intracellular protons via arginine decarboxylase is one mechanism used by P. mirabilis to conserve ΔpH and μH(+) for motility. |
format | Online Article Text |
id | pubmed-4234256 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BlackWell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-42342562014-12-04 Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force Armbruster, Chelsie E Hodges, Steven A Smith, Sara N Alteri, Christopher J Mobley, Harry L T Microbiologyopen Original Research Swarming contributes to Proteus mirabilis pathogenicity by facilitating access to the catheterized urinary tract. We previously demonstrated that 0.1–20 mmol/L arginine promotes swarming on normally nonpermissive media and that putrescine biosynthesis is required for arginine-induced swarming. We also previously determined that arginine-induced swarming is pH dependent, indicating that the external proton concentration is critical for arginine-dependent effects on swarming. In this study, we utilized survival at pH 5 and motility as surrogates for measuring changes in the proton gradient (ΔpH) and proton motive force (μH(+)) in response to arginine. We determined that arginine primarily contributes to ΔpH (and therefore μH(+)) through the action of arginine decarboxylase (speA), independent of the role of this enzyme in putrescine biosynthesis. In addition to being required for motility, speA also contributed to fitness during infection. In conclusion, consumption of intracellular protons via arginine decarboxylase is one mechanism used by P. mirabilis to conserve ΔpH and μH(+) for motility. BlackWell Publishing Ltd 2014-10 2014-08-07 /pmc/articles/PMC4234256/ /pubmed/25100003 http://dx.doi.org/10.1002/mbo3.194 Text en © 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Armbruster, Chelsie E Hodges, Steven A Smith, Sara N Alteri, Christopher J Mobley, Harry L T Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title | Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title_full | Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title_fullStr | Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title_full_unstemmed | Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title_short | Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
title_sort | arginine promotes proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4234256/ https://www.ncbi.nlm.nih.gov/pubmed/25100003 http://dx.doi.org/10.1002/mbo3.194 |
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