Jha Payal, Laskar Shyamasree, Dubey Swati, Bhattacharyya Mrinal K, Bhattacharyya Sunanda
Department of Biochemistry, School of Life Sciences, University of Hyderabad, Telangana, 500046, India.
Department of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Telangana, 500046, India.
Mol Biochem Parasitol. 2017 Jun;214:10-13. doi: 10.1016/j.molbiopara.2017.03.003. Epub 2017 Mar 18.
Out of the total forty four members of Plasmodium falciparum Hsp40 protein family, nineteen of them possess a PEXEL motif, and are predicted to be exported into the cytosol of an infected RBC. It is speculated that the human Hsp70 (hHsp70), which resides into the cytosol of the host erythrocyte, along with the exported PfHsp40s assists in the folding of parasitic proteins, thus playing a crucial role in the establishment of virulence. However, till date no experimental evidence supports this hypothesis. Our work establishes that the PEXEL motifs containing Type II PfDNAJ proteins specifically interact with hHsp70 (HSPA1A). It suggests that there exists a specific factor in PfDNAJ that determines the choice of cognate Hsp70. This opens up an interesting avenue of malaria research.
在恶性疟原虫热休克蛋白40（Hsp40）蛋白家族的总共44个成员中，其中19个具有PEXEL基序，并预计会被输出到被感染红细胞的细胞质中。据推测，存在于宿主红细胞细胞质中的人类热休克蛋白70（hHsp70）与输出的恶性疟原虫热休克蛋白40（PfHsp40）一起协助寄生虫蛋白的折叠，从而在毒力确立中发挥关键作用。然而，迄今为止尚无实验证据支持这一假设。我们的研究确定，含有PEXEL基序的II型PfDNAJ蛋白与hHsp70（HSPA1A）特异性相互作用。这表明PfDNAJ中存在一个特定因子，可决定同源热休克蛋白70的选择。这为疟疾研究开辟了一条有趣的途径。
