Novel Functions of an Iron-Sulfur Flavoprotein from Trichomonas vaginalis Hydrogenosomes

0430460 - ÚOCHB 2015 RIV US eng J - Článek v odborném periodiku
Smutná, T. - Pilařová, K. - Tarábek, Ján - Tachezy, J. - Hrdý, I.
Novel Functions of an Iron-Sulfur Flavoprotein from Trichomonas vaginalis Hydrogenosomes.
Antimicrobial Agents and Chemotherapy. Roč. 58, č. 6 (2014), s. 3224-3232. ISSN 0066-4804. E-ISSN 1098-6596
Grant ostatní: GA ČR(CZ) GC13-09208J
Institucionální podpora: RVO:61388963
Klíčová slova: Methanosarcina thermophila * nitric oxide * Trichomonas vaginalis
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 4.476, rok: 2014

Iron-sulfur flavoproteins (Isf) are flavin mononucleotide (FMN)- and FeS cluster-containing proteins commonly encountered in anaerobic prokaryotes. However, with the exception of Isf from Methanosarcina thermophila, which participates in oxidative stress management by removing oxygen and hydrogen peroxide, none of these proteins has been characterized in terms of function. Trichomonas vaginalis, a sexually transmitted eukaryotic parasite of humans, was found to express several iron-sulfur flavoprotein (TvIsf) homologs in its hydrogenosomes. We show here that in addition to having oxygen-reducing activity, the recombinant TvIsf also functions as a detoxifying reductase of metronidazole and chloramphenicol, both of which are antibiotics effective against a variety of anaerobic microbes. TvIsf can utilize both NADH and reduced ferredoxin as electron donors. Given the prevalence of Isf in anaerobic prokaryotes, we propose that these proteins are central to a novel defense mechanism against xenobiotics.
Trvalý link: http://hdl.handle.net/11104/0235560