Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i>
Replacement of the <i>Lactobacillus</i> dominated vaginal microbiome by a mixed bacterial population including <i>Prevotella bivia</i> is associated with bacterial vaginosis (BV). To understand the impact of <i>P. bivia</i> on this microbiome, its growth requireme...
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2021
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oai:doaj.org-article:174589f050bc489788c6e24cbb940c9b2021-11-11T17:20:33ZCentral Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i>10.3390/ijms2221119251422-00671661-6596https://doaj.org/article/174589f050bc489788c6e24cbb940c9b2021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11925https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Replacement of the <i>Lactobacillus</i> dominated vaginal microbiome by a mixed bacterial population including <i>Prevotella bivia</i> is associated with bacterial vaginosis (BV). To understand the impact of <i>P. bivia</i> on this microbiome, its growth requirements and mode of energy production were studied. Anoxic growth with glucose depended on CO<sub>2</sub> and resulted in succinate formation, indicating phosphoenolpyruvate carboxylation and fumarate reduction as critical steps. The reductive branch of fermentation relied on two highly active, membrane-bound enzymes, namely the quinol:fumarate reductase (QFR) and Na<sup>+</sup>-translocating NADH:quinone oxidoreductase (NQR). Both enzymes were characterized by activity measurements, in-gel fluorography, and VIS difference spectroscopy, and the Na<sup>+</sup>-dependent build-up of a transmembrane voltage was demonstrated. NQR is a potential drug target for BV treatment since it is neither found in humans nor in <i>Lactobacillus</i>. In <i>P. bivia</i>, the highly active enzymes L-asparaginase and aspartate ammonia lyase catalyze the conversion of asparagine to the electron acceptor fumarate. However, the by-product ammonium is highly toxic. It has been proposed that <i>P. bivia</i> depends on ammonium-utilizing <i>Gardnerella vaginalis</i>, another typical pathogen associated with BV, and provides key nutrients to it. The product pattern of <i>P. bivia</i> growing on glucose in the presence of mixed amino acids substantiates this notion.Lena SchleicherSebastian HerdanGünter FritzAndrej TrautmannJana SeifertJulia SteuberMDPI AGarticlebacterial vaginosis<i>Prevotella bivia</i>Na<sup>+</sup>-translocating NADH:quinone oxidoreductasefumarate reductaseamino acid degradationBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11925, p 11925 (2021) |
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bacterial vaginosis <i>Prevotella bivia</i> Na<sup>+</sup>-translocating NADH:quinone oxidoreductase fumarate reductase amino acid degradation Biology (General) QH301-705.5 Chemistry QD1-999 |
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bacterial vaginosis <i>Prevotella bivia</i> Na<sup>+</sup>-translocating NADH:quinone oxidoreductase fumarate reductase amino acid degradation Biology (General) QH301-705.5 Chemistry QD1-999 Lena Schleicher Sebastian Herdan Günter Fritz Andrej Trautmann Jana Seifert Julia Steuber Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
description |
Replacement of the <i>Lactobacillus</i> dominated vaginal microbiome by a mixed bacterial population including <i>Prevotella bivia</i> is associated with bacterial vaginosis (BV). To understand the impact of <i>P. bivia</i> on this microbiome, its growth requirements and mode of energy production were studied. Anoxic growth with glucose depended on CO<sub>2</sub> and resulted in succinate formation, indicating phosphoenolpyruvate carboxylation and fumarate reduction as critical steps. The reductive branch of fermentation relied on two highly active, membrane-bound enzymes, namely the quinol:fumarate reductase (QFR) and Na<sup>+</sup>-translocating NADH:quinone oxidoreductase (NQR). Both enzymes were characterized by activity measurements, in-gel fluorography, and VIS difference spectroscopy, and the Na<sup>+</sup>-dependent build-up of a transmembrane voltage was demonstrated. NQR is a potential drug target for BV treatment since it is neither found in humans nor in <i>Lactobacillus</i>. In <i>P. bivia</i>, the highly active enzymes L-asparaginase and aspartate ammonia lyase catalyze the conversion of asparagine to the electron acceptor fumarate. However, the by-product ammonium is highly toxic. It has been proposed that <i>P. bivia</i> depends on ammonium-utilizing <i>Gardnerella vaginalis</i>, another typical pathogen associated with BV, and provides key nutrients to it. The product pattern of <i>P. bivia</i> growing on glucose in the presence of mixed amino acids substantiates this notion. |
format |
article |
author |
Lena Schleicher Sebastian Herdan Günter Fritz Andrej Trautmann Jana Seifert Julia Steuber |
author_facet |
Lena Schleicher Sebastian Herdan Günter Fritz Andrej Trautmann Jana Seifert Julia Steuber |
author_sort |
Lena Schleicher |
title |
Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
title_short |
Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
title_full |
Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
title_fullStr |
Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
title_full_unstemmed |
Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen <i>Prevotella bivia</i> |
title_sort |
central carbon metabolism, sodium-motive electron transfer, and ammonium formation by the vaginal pathogen <i>prevotella bivia</i> |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/174589f050bc489788c6e24cbb940c9b |
work_keys_str_mv |
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_version_ |
1718432103162445824 |