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Peroxiredoxins in Parasites

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This is the publisher’s final pdf. The published article is copyrighted by Mary Ann Liebert, Inc. and can be found at: http://www.liebertpub.com/.Significance: Parasite survival and virulence relies on effective defenses against reactive oxygen and nitrogen species produced by the host immune system. Peroxiredoxins (Prxs) are ubiquitous enzymes now thought to be central to such defenses and, as such, have potential value as drug targets and vaccine antigens. Recent Advances: Plasmodial and kinetoplastid Prx systems are the most extensively studied, yet remain inadequately understood. For many other parasites our knowledge is even less well developed. Through parasite genome sequencing efforts, however, the key players are being discovered and characterized. Here we describe what is known about the biochemistry, regulation, and cell biology of Prxs in parasitic protozoa, helminths, and fungi. At least one Prx is found in each parasite with a sequenced genome, and a notable theme is the common patterns of expression, localization, and functionality among sequence-similar Prxs in related species. Critical Issues: The nomenclature of Prxs from parasites is in a state of disarray, causing confusion and making comparative inferences difficult. Here we introduce a systematic Prx naming convention that is consistent between organisms and informative about structural and evolutionary relationships. Future Directions: The new nomenclature should stimulate the crossfertilization of ideas among parasitologists and with the broader redox research community. The diverse parasite developmental stages and host environments present complex systems in which to explore the variety of roles played by Prxs, with a view toward parlaying what is learned into novel therapies and vaccines that are urgently needed. Antioxid. Redox Signal. 17, 608-633

Topics: Thiol specific antioxidant, Redox sensitive oligomerization, Schistosoma mansoni thioredoxin, Protozoan trichomonas vaginalis, Falciparum 1 Cys Peroxiredoxin, Alkyl hydroperoxide reductase, One conserved cysteine, Amebic liver abscess, Entamoeba histolytica, Plasmodium falciparum
Publisher: Mary Ann Liebert, Inc.
Year: 2012
DOI identifier: 10.1089/ars.2011.4404
OAI identifier: oai:ir.library.oregonstate.edu:1957/42278
Provided by: ScholarsArchive@OSU
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