a plasmodium falciparum host-targeting motif functions in export during blood stage infection of the rodent malarial parasite plasmodium berghei恶性疟原虫host-targeting主题函数导出血液阶段啮齿动物疟原虫感染鼠.pdfVIP
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a plasmodium falciparum host-targeting motif functions in export during blood stage infection of the rodent malarial parasite plasmodium berghei恶性疟原虫host-targeting主题函数导出血液阶段啮齿动物疟原虫感染鼠
A Plasmodium falciparum Host-Targeting Motif
Functions in Export during Blood Stage Infection of the
Rodent Malarial Parasite Plasmodium berghei
. ´ ´ . .
Julia J. MacKenzie , Noe D. Gomez , Souvik Bhattacharjee , Shaina Mann, Kasturi Haldar*
Department of Pathology and Microbiology-Immunology, Northwestern University, Feinberg School of Medicine, Chicago, Illinois, United States of America
Abstract
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.
´
Citation: MacKenzie JJ, Gomez ND, Bhattacharjee S, Mann S, Haldar K (2008) A Plasmodium falciparum Host-Targeting Motif Functions in Export during Blood
Stage Infection of the Rodent Malarial Parasite Plasmodium berghei. PLoS ONE 3
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