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Heterologous expression of plasmodial proteins for structural studies and functional annotation

Birkholtz, L and Blatch, Gregory L and Coetzer, T and Hoppe, H and Human, E and Morris, E and Ngcete, Z and Oldfield, L and Roth, R and Shonhai, A and Stephens, L and Louw, A (2008) Heterologous expression of plasmodial proteins for structural studies and functional annotation. Malaria Journal, 7 (1). ISSN 1475-2875

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Abstract

Malaria remains the world's most devastating tropical infectious disease with as many as 40% of the world population living in risk areas. The widespread resistance of Plasmodium parasites to the cost-effective chloroquine and antifolates has forced the introduction of more costly drug combinations, such as Coartem®. In the absence of a vaccine in the foreseeable future, one strategy to address the growing malaria problem is to identify and characterize new and durable antimalarial drug targets, the majority of which are parasite proteins. Biochemical and structure-activity analysis of these proteins is ultimately essential in the characterization of such targets but requires large amounts of functional protein. Even though heterologous protein production has now become a relatively routine endeavour for most proteins of diverse origins, the functional expression of soluble plasmodial proteins is highly problematic and slows the progress of antimalarial drug target discovery. Here the status quo of heterologous production of plasmodial proteins is presented, constraints are highlighted and alternative strategies and hosts for functional expression and annotation of plasmodial proteins are reviewed.

Item Type: Article
Uncontrolled Keywords: ResPubID22199. malaria, plasmodium parasites, proteins
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 1108 Medical Microbiology
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Depositing User: VUIR
Date Deposited: 19 Apr 2012 23:32
Last Modified: 19 Apr 2012 23:32
URI: http://vuir.vu.edu.au/id/eprint/8145
DOI: 10.1186/1475-2875-7-197
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Citations in Scopus: 30 - View on Scopus

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