A Plasmodium falciparum host-targeting motif functions in export during blood stage infection of the rodent malarial parasite Plasmodium berghei.
Plasmodium falciparum (P. falciparum) secretes hundreds of proteins--including major virulence proteins--into the host erythrocyte. In order to reach the host cytoplasm, most P. falciparum proteins contain an N terminal host-targeting (HT) motif composed of 11 amino acids. In silico analyses have suggested that the HT motif is conserved throughout the Plasmodium species but experimental evidence only exists for P. falciparum. Here, we show that in the rodent malaria parasite Plasmodium berghei (P. berghei) a reporter-like green fluorescent protein expressed by the parasite can be exported to the erythrocyte cytoplasm in a HT-specific manner. This provides the first experimental proof that the HT motif can function as a signal for protein delivery to the erythrocyte across Plasmodium species. Further, it suggests that P. berghei may serve as a model for validation of P. falciparum secretome proteins. We also show that tubovesicular membranes extend from the vacuolar parasite into the erythrocyte cytoplasm and speculate that these structures may facilitate protein export to the erythrocyte.
Department of Pathology and Microbiology-Immunology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, United States of America.
Julia J
JJ
MacKenzie
Noé D
ND
Gómez
Souvik
S
Bhattacharjee
Shaina
S
Mann
Kasturi
K
Haldar
D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D049452:Green Fluorescent Proteins / Q000235:genetics; D008288:Malaria / Q000097:blood* / Q000503:physiopathology; D051379:Mice; D008807:Mice, Inbred BALB C; D010962:Plasmodium berghei / Q000502:physiology*; D010963:Plasmodium falciparum / Q000502:physiology*; D019076:Transgenes
D017931:DNA Primers; D049452:Green Fluorescent Proteins