Potential Interaction of Plasmodium falciparum Hsp60 and Calpain
The Korean Journal of Parasitology
;
: 665-673, 2015.
Artigo
em Inglês
| WPRIM
| ID: wpr-9589
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Plasmodium falciparum
/
Ligação Proteica
/
Dados de Sequência Molecular
/
Calpaína
/
Proteínas de Protozoários
/
Alinhamento de Sequência
/
Sequência de Aminoácidos
/
Malária Falciparum
/
Chaperonina 60
/
Eritrócitos
Limite:
Humanos
Idioma:
Inglês
Revista:
The Korean Journal of Parasitology
Ano de publicação:
2015
Tipo de documento:
Artigo
Similares
MEDLINE
...
LILACS
LIS