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Catestatin, an endogenous chromogranin A-derived peptide, inhibits in vitro growth of Plasmodium falciparum.

Authors :
Akaddar A
Doderer-Lang C
Marzahn MR
Delalande F
Mousli M
Helle K
Van Dorsselaer A
Aunis D
Dunn BM
Metz-Boutigue MH
Candolfi E
Source :
Cellular and molecular life sciences : CMLS [Cell Mol Life Sci] 2010 Mar; Vol. 67 (6), pp. 1005-15. Date of Electronic Publication: 2009 Dec 31.
Publication Year :
2010

Abstract

Catestatin, an endogenous peptide derived from bovine chromogranin A, and its active domain cateslytin display powerful antimicrobial activities. We have tested the activities of catestatin and other related peptides on the growth of Plasmodium falciparum in vitro. Catestatin inhibits growth of the chloroquine-sensitive strain of P. falciparum 3D7, exhibiting 88% inhibition at 20 microM. A similar partial inhibition of parasite growth was observed for the chloroquine-resistant strain, 7G8 (64%,) and the multidrug-resistant strain, W2 (62%). In the presence of parasite-specific lactate dehydrogenase, a specific protein-protein interaction between catestatin and plasmepsin II precursor was demonstrated. In addition, catestatin partially inhibited the parasite-specific proteases plasmepsin in vitro. A specific interaction between catestatin and plasmepsins II and IV from P. falciparum and plasmepsin IV from the three remaining species of Plasmodium known to infect man was observed, suggesting a catestatin-induced reduction in availability of nutrients for protein synthesis in the parasite.

Details

Language :
English
ISSN :
1420-9071
Volume :
67
Issue :
6
Database :
MEDLINE
Journal :
Cellular and molecular life sciences : CMLS
Publication Type :
Academic Journal
Accession number :
20043183
Full Text :
https://doi.org/10.1007/s00018-009-0235-8