Potential Interaction of Plasmodium falciparum Hsp60 and Calpain.
10.3347/kjp.2015.53.6.665
- Author:
Seon Ju YEO
1
;
Dong Xu LIU
;
Hyun PARK
Author Information
1. Zoonosis Research Center, Department of Infection Biology, School of Medicine, Wonkwang University, Iksan 54538, Korea. hyunpk@wku.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Plasmodium falciparum;
heat shock protein 60;
calpain;
mizoribine
- MeSH:
Amino Acid Sequence;
Calpain/genetics/*metabolism;
Chaperonin 60/chemistry/genetics/*metabolism;
Erythrocytes/parasitology;
Humans;
Malaria, Falciparum/parasitology;
Molecular Sequence Data;
Plasmodium falciparum/chemistry/enzymology/genetics/*metabolism;
Protein Binding;
Protozoan Proteins/chemistry/genetics/*metabolism;
Sequence Alignment
- From:The Korean Journal of Parasitology
2015;53(6):665-673
- CountryRepublic of Korea
- Language:English
-
Abstract:
After invasion of red blood cells, malaria matures within the cell by degrading hemoglobin avidly. For enormous protein breakdown in trophozoite stage, many efficient and ordered proteolysis networks have been postulated and exploited. In this study, a potential interaction of a 60-kDa Plasmodium falciparum (Pf)-heat shock protein (Hsp60) and Pf-calpain, a cysteine protease, was explored. Pf-infected RBC was isolated and the endogenous Pf-Hsp60 and Pf-calpain were determined by western blot analysis and similar antigenicity of GroEL and Pf-Hsp60 was determined with anti-Pf-Hsp60. Potential interaction of Pf-calpain and Pf-Hsp60 was determined by immunoprecipitation and immunofluorescence assay. Mizoribine, a well-known inhibitor of Hsp60, attenuated both Pf-calpain enzyme activity as well as P. falciparum growth. The presented data suggest that the Pf-Hsp60 may function on Pf-calpain in a part of networks during malaria growth.
