Proteomic analysis of exported chaperone/co－chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions

ABSTRACT: Project describe: The P. falciparum export 300-400 proteins during infect human red blood cell, where they are involved in host cell modification including We recently identified a novel structure in P. falciparum-infected erythrocytes which we refer to as J-dots. These structures contain exported parasite-encoded Hsp40s and are implicated in protein transport through the erythrocyte. This project wants isolation and proteomic characterisation of parasite-induced intra-erythrocytic structure to understand their importance in parasite survival and virulence. A more thorough understanding of this novel process may eventually lead to new avenues for therapy.

INSTRUMENT(S):

ORGANISM(S): Plasmodium Falciparum Homo Sapiens (human)

TISSUE(S): Blood Cell, Cell Culture, Blood

DISEASE(S): Plasmodium Falciparum Malaria

SUBMITTER: Qi Zhang  

LAB HEAD: Jude M. Przyborski

PROVIDER: PXD003789 | Pride | 2018-10-18

REPOSITORIES: Pride