Protein Cysteine S-Nitrosylation Provides Reducing Power by Enhancing Lactate Dehydrogenase Activity in Trichomonas Vaginalis Under Iron Deficiency
| العنوان: | Protein Cysteine S-Nitrosylation Provides Reducing Power by Enhancing Lactate Dehydrogenase Activity in Trichomonas Vaginalis Under Iron Deficiency |
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| المؤلفون: | Kuo-Yang Huang, Fu-Man Ku, Cheng-Hsun Chiu, Po-Jung Huang, Yuan-Ming Yeh, Chi-Ching Lee, Petrus Tang, Seow-Chin Ong, Wei-Hung Cheng, Rose Lin |
| المصدر: | Parasites & Vectors Parasites & Vectors, Vol 13, Iss 1, Pp 1-14 (2020) |
| بيانات النشر: | Research Square Platform LLC, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Iron, Protozoan Proteins, Dehydrogenase, Nicotinamide adenine dinucleotide, Biology, Nitric Oxide, Cysteine S-nitrosylation, lcsh:Infectious and parasitic diseases, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Lactate dehydrogenase, Pyruvic Acid, medicine, Trichomonas vaginalis, lcsh:RC109-216, Glycolysis, Cysteine, L-Lactate Dehydrogenase, Protein nitrosylation, Research, Iron deficiency, S-Nitrosylation, NAD, medicine.disease, 030104 developmental biology, Infectious Diseases, chemistry, Biochemistry, Parasitology, NAD+ kinase, Oxidation-Reduction, 030217 neurology & neurosurgery, Protein Modification, Translational |
| الوصف: | BackgroundIron plays essential roles in the pathogenesis and proliferation ofTrichomonas vaginalis, the causative agent of the most prevalent non-viral human sexually transmitted infection. We previously demonstrated that under iron deficiency, the endogenous nitric oxide (NO) is accumulated and capable of regulating the survival ofT. vaginalis. Herein, we aim to explore the influence of NO on the activity of the pyruvate-reducing enzyme lactate dehydrogenase inT. vaginalis(TvLDH).MethodsLevels of lactate and pyruvate were detected for determining glycolysis activity inT. vaginalisunder iron deficiency. Quantitative PCR was performed to determine the expression of TvLDH. S-nitrosylated (SNO) proteomics was conducted to identify the NO-modified proteins. The activities of glyceraldehyde-3-phosphate dehydrogenase (TvGAPDH) and TvLDH were measured after sodium nitrate treatment. The effects of protein nitrosylation on the production of cellular reducing power were examined by measuring the amount of nicotinamide adenine dinucleotide (NAD) and the ratio of the NAD redox pair (NAD+/NADH).ResultsWe found that although the glycolytic pathway was activated in cells under iron depletion, the level of pyruvate was decreased due to the increased level of TvLDH. By analyzing the SNO proteome ofT. vaginalisupon iron deficiency, we found that TvLDH is one of the glycolytic enzymes modified by SNO. The production of pyruvate was significantly reduced after nitrate treatment, indicating that protein nitrosylation accelerated the consumption of pyruvate by increasing TvLDH activity. Nitrate treatment also induced NAD oxidation, suggesting that protein nitrosylation was the key posttranslational modification controlling cellular redox status.ConclusionsWe demonstrated that NO-mediated protein nitrosylation plays pivotal roles in the regulation of glycolysis, pyruvate metabolism, and the activity of TvLDH. The recycling of oxidized NAD catalyzed by TvLDH provided the reducing power that allowedT. vaginalisto adapt to the iron-deficient environment. |
| DOI: | 10.21203/rs.3.rs-33221/v1 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f0caf422a932d9a3e3be985e285d563 https://doi.org/10.21203/rs.3.rs-33221/v1 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....4f0caf422a932d9a3e3be985e285d563 |
| قاعدة البيانات: | OpenAIRE |
| DOI: | 10.21203/rs.3.rs-33221/v1 |
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