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© Research
Publication : Cellular microbiology

The Plasmodium translocon of exported proteins component EXP2 is critical for establishing a patent malaria infection in mice

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cellular microbiology - 14 Oct 2015

Kalanon M, Bargieri D, Sturm A, Matthews K, Ghosh S, Goodman CD, Thiberge S, Mollard V, McFadden GI, Ménard R, de Koning-Ward TF

Link to Pubmed [PMID] – 26347246

Cell. Microbiol. 2016 Mar;18(3):399-412

Export of most malaria proteins into the erythrocyte cytosol requires the Plasmodium translocon of exported proteins (PTEX) and a cleavable Plasmodium export element (PEXEL). In contrast, the contribution of PTEX in the liver stages and export of liver stage proteins is unknown. Here, using the FLP/FRT conditional mutatagenesis system, we generate transgenic Plasmodium berghei parasites deficient in EXP2, the putative pore-forming component of PTEX. Our data reveal that EXP2 is important for parasite growth in the liver and critical for parasite transition to the blood, with parasites impaired in their ability to generate a patent blood-stage infection. Surprisingly, whilst parasites expressing a functional PTEX machinery can efficiently export a PEXEL-bearing GFP reporter into the erythrocyte cytosol during a blood stage infection, this same reporter aggregates in large accumulations within the confines of the parasitophorous vacuole membrane during hepatocyte growth. Notably HSP101, the putative molecular motor of PTEX, could not be detected during the early liver stages of infection, which may explain why direct protein translocation of this soluble PEXEL-bearing reporter or indeed native PEXEL proteins into the hepatocyte cytosol has not been observed. This suggests that PTEX function may not be conserved between the blood and liver stages of malaria infection.

https://www.ncbi.nlm.nih.gov/pubmed/26347246