The three NADH dehydrogenases of Pseudomonas aeruginosa: Their roles in energy metabolism and links to virulence
Pseudomonas aeruginosa is a ubiquitous opportunistic pathogen which relies on a highly adaptable metabolism to achieve broad pathogenesis. In one example of this flexibility, to catalyze the NADH:quinone oxidoreductase step of the respiratory chain, P. aeruginosa has three different enzymes: NUO, NQ...
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Published in: | PloS one Vol. 16; no. 2; p. e0244142 |
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Main Authors: | , , , , , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Public Library of Science
03-02-2021
Public Library of Science (PLoS) |
Subjects: | |
Online Access: | Get full text |
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Summary: | Pseudomonas aeruginosa is a ubiquitous opportunistic pathogen which relies on a highly adaptable metabolism to achieve broad pathogenesis. In one example of this flexibility, to catalyze the NADH:quinone oxidoreductase step of the respiratory chain, P. aeruginosa has three different enzymes: NUO, NQR and NDH2, all of which carry out the same redox function but have different energy conservation and ion transport properties. In order to better understand the roles of these enzymes, we constructed two series of mutants: (i) three single deletion mutants, each of which lacks one NADH dehydrogenase and (ii) three double deletion mutants, each of which retains only one of the three enzymes. All of the mutants grew approximately as well as wild type, when tested in rich and minimal medium and in a range of pH and [Na+] conditions, except that the strain with only NUO (ΔnqrFΔndh) has an extended lag phase. During exponential phase, the NADH dehydrogenases contribute to total wild-type activity in the following order: NQR > NDH2 > NUO. Some mutants, including the strain without NQR (ΔnqrF) had increased biofilm formation, pyocyanin production, and killed more efficiently in both macrophage and mouse infection models. Consistent with this, ΔnqrF showed increased transcription of genes involved in pyocyanin production. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Department of Chemical, Paper and Biomedical Engineering, Miami University, Oxford, OH, United States of America Competing Interests: The authors have declared that no competing interests exist. Current address: Department of Chemical Engineering and Pharmaceutical Technology, Universidad de La Laguna, Tenerife, Spain Current address: Abbott, Abbott Park, IL, United States of America Current address: Department of Pediatrics, Washington University School of Medicine, St. Louis, MO, United States of America |
ISSN: | 1932-6203 1932-6203 |
DOI: | 10.1371/journal.pone.0244142 |