Identification of an exported heat shock protein 70 in Plasmodium falciparum

Parasite

Shatakshi RanadeUtpal Tatu¹  Shweta Chaubey¹  Manish Grover¹ 

[1] Department of Biochemistry, Indian Institute of Science,Bangalore 560012,Karnataka,India

关键词: Trafficking;    Export;    Hsp70;    Chaperone;    Plasmodium falciparum;   

Others  :  808662
DOI  :  doi:10.1051/parasite/2012002

 received in 2012-10-17, accepted in 2012-10-26,  发布年份 2013

【 摘 要 】

Host cell remodelling is a hallmark of malaria pathogenesis. It involves protein folding, unfolding and trafficking events and thus participation of chaperones such as Hsp70s and Hsp40s is well speculated. Until recently, only Hsp40s were thought to be the sole representative of the parasite chaperones in the exportome. However, based on the re-annotated Plasmodium falciparum genome sequence, a putative candidate for exported Hsp70 has been reported, which otherwise was known to be a pseudogene. We raised a specific antiserum against a C-terminal peptide uniquely present in PfHsp70-x. Immunoblotting and immunofluorescence-based approaches in combination with sub-cellular fractionation by saponin and streptolysin-O have been taken to determine the expression and localization of PfHsp70-x in infected erythrocyte. The re-annotated sequence of PfHsp70-x reveals it to be a functional protein with an endoplasmic reticulum signal peptide. It gets maximally expressed at the schizont stage of intra-erythrocytic life cycle. Majority of the protein localizes to the parasitophorous vacuole and some of it gets exported to the erythrocyte compartment where it associates with Maurer’s clefts. The identification of an exported parasite Hsp70 chaperone presents us with the fact that the parasite has evolved customized chaperones which might be playing crucial roles in aspects of trafficking and host cell remodelling.

【 授权许可】

   
© M. Grover et al., published by EDP Sciences, 2013

【 图 表 】

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