Peroxiredoxins (Prxs) are ubiquitary proteins able to play multiple physiological roles, that include thiol-dependent peroxidase, chaperone holdase, sensor of H2O2, regulator of H2O2-dependent signal cascades, and modulator of the immune response. Prxs have been found in a great number of human pathogens, both eukaryotes and prokaryotes. Gene knock-out studies demonstrated that Prxs are essential for the survival and virulence of at least some of the pathogens tested, making these proteins potential drug targets. However, the multiplicity of roles played by Prxs constitutes an unexpected obstacle to drug development. Indeed, selective inhibitors of some of the functions of Prxs are known (namely of the peroxidase and holdase functions) and are here reported. However, it is often unclear which function is the most relevant in each pathogen, hence which one is most desirable to inhibit. Indeed there are evidences that the main physiological role of Prxs may not be the same in different parasites. We here review which functions of Prxs have been demonstrated to be relevant in different human parasites, finding that the peroxidase and chaperone activities figure prominently, whereas other known functions of Prxs have rarely, if ever, been observed in parasites, or have largely escaped detection thus far.

Typical 2-cys peroxiredoxins in human parasites: several physiological roles for a potential chemotherapy target / Angelucci, Francesco; Miele, Adriana Erica; Ardini, Matteo; Boumis, Giovanna; Saccoccia, Fulvio; Bellelli, Andrea. - In: MOLECULAR AND BIOCHEMICAL PARASITOLOGY. - ISSN 0166-6851. - STAMPA. - 206:1-2(2016), pp. 2-12. [10.1016/j.molbiopara.2016.03.005]

Typical 2-cys peroxiredoxins in human parasites: several physiological roles for a potential chemotherapy target

MIELE, Adriana Erica;BOUMIS, Giovanna;BELLELLI, Andrea
2016

Abstract

Peroxiredoxins (Prxs) are ubiquitary proteins able to play multiple physiological roles, that include thiol-dependent peroxidase, chaperone holdase, sensor of H2O2, regulator of H2O2-dependent signal cascades, and modulator of the immune response. Prxs have been found in a great number of human pathogens, both eukaryotes and prokaryotes. Gene knock-out studies demonstrated that Prxs are essential for the survival and virulence of at least some of the pathogens tested, making these proteins potential drug targets. However, the multiplicity of roles played by Prxs constitutes an unexpected obstacle to drug development. Indeed, selective inhibitors of some of the functions of Prxs are known (namely of the peroxidase and holdase functions) and are here reported. However, it is often unclear which function is the most relevant in each pathogen, hence which one is most desirable to inhibit. Indeed there are evidences that the main physiological role of Prxs may not be the same in different parasites. We here review which functions of Prxs have been demonstrated to be relevant in different human parasites, finding that the peroxidase and chaperone activities figure prominently, whereas other known functions of Prxs have rarely, if ever, been observed in parasites, or have largely escaped detection thus far.
2016
Chaperone holdase; leishmaniasis; malaria; peroxiredoxin; schistosomiasis; thioredoxin-dependent peroxidase; toxoplasmosis; trypanosomiasis; molecular biology; parasitology
01 Pubblicazione su rivista::01a Articolo in rivista
Typical 2-cys peroxiredoxins in human parasites: several physiological roles for a potential chemotherapy target / Angelucci, Francesco; Miele, Adriana Erica; Ardini, Matteo; Boumis, Giovanna; Saccoccia, Fulvio; Bellelli, Andrea. - In: MOLECULAR AND BIOCHEMICAL PARASITOLOGY. - ISSN 0166-6851. - STAMPA. - 206:1-2(2016), pp. 2-12. [10.1016/j.molbiopara.2016.03.005]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/954529
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