Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force
Article first published online: 7 AUG 2014
© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.
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.
Volume 3, Issue 5, pages 630–641, October 2014
How to Cite
MicrobiologyOpen 2014; 3(5): 630–641
- Issue published online: 9 OCT 2014
- Article first published online: 7 AUG 2014
- Manuscript Accepted: 16 JUN 2014
- Manuscript Revised: 4 JUN 2014
- Manuscript Received: 14 APR 2014
- National Institute of Allergy and Infectious Diseases
- National Institutes of Health. Grant Numbers: R01AI059722, F32AI102552
- Arginine decarboxylase;
- Proteus mirabilis ;
- 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 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.