title: Antioxidant defence systems in the protozoan pathogen Giardia intestinalis.
abstract: The microaerophilic protist Giardia intestinalis is the causative agent of giardiasis, one of the most common intestinal infectious diseases worldwide. The pathogen lacks not only respiratory terminal oxidases (being amitochondriate), but also several conventional antioxidant enzymes, including catalase, superoxide dismutase and glutathione peroxidase. In spite of this, since living attached to the mucosa of the proximal small intestine, the parasite should rely on an efficient antioxidant system to survive the oxidative and nitrosative stress conditions found in this tract of the human gut. Here, we review current knowledge on the antioxidant defence systems in G. intestinalis, focusing on the progress made over the last decade in the field. The relevance of this research and future perspectives are discussed.
authors.affiliation: Department of Biochemical Sciences and Istituto Pasteur-Cenci Bolognetti, Sapienza University of Rome, Italy; CNR Institute of Molecular Biology and Pathology, Rome, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Mastronicola
authors.affiliation: Department of Biochemical Sciences and Istituto Pasteur-Cenci Bolognetti, Sapienza University of Rome, Italy.
authors.forename: Micol
authors.initials: M
authors.lastname: Falabella
authors.affiliation: Department of Biochemical Sciences and Istituto Pasteur-Cenci Bolognetti, Sapienza University of Rome, Italy.
authors.forename: Elena
authors.initials: E
authors.lastname: Forte
authors.affiliation: Department of Biochemical Sciences and Istituto Pasteur-Cenci Bolognetti, Sapienza University of Rome, Italy.
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Testa
authors.affiliation: Department of Biochemical Sciences and Istituto Pasteur-Cenci Bolognetti, Sapienza University of Rome, Italy.
authors.forename: Paolo
authors.initials: P
authors.lastname: Sarti
authors.affiliation: CNR Institute of Molecular Biology and Pathology, Rome, Italy. Electronic address: alessandro.giuffre@uniroma1.it.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Giuffrè
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000378:metabolism; D005420:Flavoproteins / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D016829:Giardia lamblia / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D005873:Giardiasis / Q000469:parasitology / Q000473:pathology; D006420:Hemeproteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D054464:Peroxiredoxins / Q000235:genetics / Q000378:metabolism*; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000975:Antioxidants; D005420:Flavoproteins; D006420:Hemeproteins; D009097:Multienzyme Complexes; D015800:Protozoan Proteins; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; C121849:superoxide reductase; D054464:Peroxiredoxins; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases
keywords: Anaerobic protozoa; Drug targets; Enzymatic detoxification; Intestinal infectious diseases; Oxidative and nitrosative stress; Recombinant enzymes