Plasmodium falciparum J-dot localized J domain protein A8iJp modulates the chaperone activity of human HSPA8.
FEBS Lett
; 598(7): 818-836, 2024 Apr.
Article
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| MEDLINE
| ID: mdl-38418371
ABSTRACT
Plasmodium falciparum renovates the host erythrocyte to survive during intraerythrocytic development. This renovation requires many parasite proteins to unfold and move outside the parasitophorous vacuolar membrane, and chaperone-regulated protein folding becomes essential for the exported proteins to function. We report on a type-IV J domain protein (JDP), PF3D7_1401100, which we found to be processed before export and trafficked inside the lumen of parasite-derived structures known as J-dots. We found this protein to have holdase activity, as well as stimulate the ATPase and aggregation suppression activity of the human HSP70 chaperone HsHSPA8; thus, we named it "HSPA8-interacting J protein" (A8iJp). Moreover, we found a subset of HsHSPA8 to co-localize with A8iJp inside the infected human erythrocyte. Our results suggest that A8iJp modulates HsHSPA8 chaperone activity and may play an important role in host erythrocyte renovation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Plasmodium falciparum
/
Proteínas del Choque Térmico HSP40
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2024
Tipo del documento:
Article
País de afiliación:
India