期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 67, 期 6, 页码 1005-1015出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0235-8
关键词
Plasmodium falciparum; Antimicrobial peptide; Catestatin; Cateslytin; Chromogranin A; Plasmepsins II and IV
资金
- Inserm [U575]
- Universite de Strasbourg (France)
- CNRS, le Ministere de la Recherche et de l'Education
- les Hopitaux Universitaires de Strasbourg
- Region Alsace
- National Institutes of Health
- Veterans Affairs, USA
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 mu M. 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.
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