gms | German Medical Science

10th Malaria Meeting

Working party Malaria / Section Antiparasitic Chemotherapy of the Paul-Ehrlich-Society (PEG e.V.) in cooperation with the German Society for Tropical Medicine and International Health (DTG e.V.) and the German Society for Parasitology (DGP e.V.)

09.11. - 10.11.2012, Marburg an der Lahn

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Hsp70, an important cog in the malaria parasite’s protein folding machinery

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  • A. Shonhai - Department of Biochemistry and Microbiology, Zululand University, KwaDlangezwa, South Africa

10th Malaria Meeting. Marburg, 09.-10.11.2012. Düsseldorf: German Medical Science GMS Publishing House; 2013. Doc12mal13

doi: 10.3205/12mal13, urn:nbn:de:0183-12mal136

Published: January 8, 2013

© 2013 Shonhai.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc-nd/3.0/deed.en). You are free: to Share – to copy, distribute and transmit the work, provided the original author and source are credited.

Outline

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Heat shock proteins (Hsps) play a central role as part of the cell’s molecular chaperone machinery. Hsp70s are proteins that are characterized by a highly conserved ATPase domain and a peptide binding domain (PBD). Hsp70 is capable of binding hydrophobic patches that are displayed by misfolded proteins. This allows it to stabilize unfolded proteins, facilitating their refolding. Plasmodium falciparum encodes 6 Hsp70s which are located in various cellular organelles. This report analyses the specialized roles of these proteins and discusses their central role in protein folding in the malaria parasite. Plasmodium falciparum Hsp70-1 (PfHsp70-1), is a stress-inducible cytosol/nuclear localized protein. Evidence for the chaperone role of this protein is presented. Furthermore, insights into its interaction with other molecular chaperones and co-chaperones such as PfHsp90, and Hsp40 co-chaperones will be discussed.