alexa Pathophysiology of Plasmodium falciparum-Infected Erythrocytes and Thiol- Mediated Antioxidant Detoxification Systems | OMICS International | Abstract
ISSN: 2470-6965

Malaria Control & Elimination
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Review Article

Pathophysiology of Plasmodium falciparum-Infected Erythrocytes and Thiol- Mediated Antioxidant Detoxification Systems

Paul Chikezie*

Department of Biochemistry, Imo State University, Owerri, Nigeria

*Corresponding Author:
Paul Chikezie
Department of Biochemistry
Imo State University
Owerri, Nigeria
Tel: +2348038935327
E-mail: [email protected]

Received Date: September 09, 2015; Accepted Date: November 05, 2015; Published Date: November 12, 2015

Citation: Chikezie P (2015) Pathophysiology of Plasmodium falciparum-Infected Erythrocytes and Thiol-Mediated Antioxidant Detoxification Systems. Malar Cont Elimination S1:003. doi: 10.4172/2470-6965.1000S1-003

Copyright: © 2015 Chikezie P. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Five species of intracellular protozoa of the genus Plasmodium cause malaria in human. The present review briefly highlighted the pathophysiology of Plasmodium falciparum infected erythrocyte and thiol-mediated antioxidant detoxification systems of P. falciparum that are required for survival of the malarial parasite in hyperoxidative intracellular environment. Scientific search engines such as PubMed, Pubget, Medline, EMBASE, Google Scholar, ScienceDirect and SpringerLink were used to retrieve online publications from 1976 to 2015. Haemoglobin that is taken up by the parasites into their acid food vacuole leads to the spontaneous oxidation of haem iron from Fe2+ to Fe3+, formation of superoxide radicals (O2•−), and subsequently, hydrogen peroxide (H2O2) and hydroxyl radicals (•− OH), which are highly reactive and cytotoxic oxygen intermediates. Additionally, toxic haem (ferri/ferroprotoporhyrin IX (FPIX) that is released upon haemoglobin digestion is biomineralized to form inert haemozoin. P. falciparum reduced glutathione (PfGSH) is a cofactor for glutathione enzyme systems and mediates in direct reductive detoxification of the toxic byproduct of haemoglobin digestion-FPIX. The postulated role of P. falciparum glutathione S-transferase (PfGST) in the development of drug resistance in malarial parasites is still being controversially discussed. However, selective inhibition of PfGST and P. falciparum thioredoxin reductase (PfTrxR) identifies novel drug targets and potential chemotherapeutic strategy to combat malaria.

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