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New Export Pathway in Plasmodium falciparum ‐Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC
Author(s) -
Mbengue Alassane,
Vialla Emilie,
Berry Laurence,
Fall Gamou,
Audiger Nicolas,
DemettreVerceil Edith,
Boteller David,
BraunBreton Catherine
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12266
Subject(s) - biology , plasmodium falciparum , chaperonin , cytoplasm , parasite hosting , membrane protein , chaperone (clinical) , microbiology and biotechnology , virulence , biochemistry , protein folding , malaria , membrane , gene , immunology , medicine , pathology , world wide web , computer science
The malaria parasite type II chaperonin PfTRiC is exported to the host erythrocyte cytoplasm and translocates unfolded parasite proteins from the parasitophorous vacuole to the membrane of Maurer's clefts. Since some of these exported proteins have the PEXEL export signature, the PfTRiC cargos likely use the PTEX translocon to pass through the parasitophorous vacuole membrane. Detection of PfTRiC in the parasitophorous vacuole lumen suggests a role for this chaperonin in the export of parasite proteins through different compartments.