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FEBS Open Bio. 2017 Dec 31;8(2):177-188. doi: 10.1002/2211-5463.12351. eCollection 2018 Feb.

A putative RNA binding protein from Plasmodium vivax apicoplast.

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Instituto de Investigaciones Químicas (IIQ) Centro de Investigaciones Científicas Isla de la Cartuja (cicCartuja) Universidad de Sevilla Consejo Superior de Investigaciones Científicas (CSIC) Sevilla Spain.
King's College London Randall Division of Cell & Molecular Biophysics London UK.


Malaria is caused by Apicomplexa protozoans from the Plasmodium genus entering the bloodstream of humans and animals through the bite of the female mosquitoes. The annotation of the Plasmodium vivax genome revealed a putative RNA binding protein (apiRBP) that was predicted to be trafficked into the apicoplast, a plastid organelle unique to Apicomplexa protozoans. Although a 3D structural model of the apiRBP corresponds to a noncanonical RNA recognition motif with an additional C-terminal α-helix (α3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α3. Hence, we used a C-terminal GFP-fused chimera to stabilize the highly insoluble apiRBP and determined its ability to bind U-rich stretches of RNA. The affinity of apiRBP toward such RNAs is highly dependent on ionic strength, suggesting that the apiRBP-RNA complex is driven by electrostatic interactions. Altogether, apiRBP represents an attractive tool for apicoplast transcriptional studies and for antimalarial drug design.


apicoplast RNA binding protein; malarial Plasmodium parasite; protein aggregation

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