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Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum.

Abstract : The ability of the malaria parasite, Plasmodium falciparum, to proliferate within the human host depends on its invasion of erythrocytes. Erythrocyte binding-like (EBL) proteins play crucial roles in the attachment of merozoites to human erythrocytes by binding to specific receptors on the cell surface. In this study, we have carried out a bioinformatics analysis of the three EBL proteins EBA-140, EBA-175 and EBA-181 and show that they contain a large amount of intrinsic disorder in particular within the RIII-V domains. The functional role of these domains has so far not been identified, although antibodies raised against these regions were shown to inhibit parasite invasion. Here, we obtain a more complete structural and dynamic view of the EBL proteins by focusing on the biophysical characterization of a smaller construct of the RIII-V regions of EBA-181 (EBA-181945-1097). We show using a number of techniques that EBA-181945-1097 is intrinsically disordered, and we obtain a detailed structural and dynamic characterization of the protein at atomic resolution using nuclear magnetic resonance (NMR) spectroscopy. Our results show that EBA-181945-1097 is essentially a statistical coil with the presence of several turn motifs and does not possess transiently populated secondary structures as is common for many intrinsically disordered proteins that fold via specific, pre-formed molecular recognition elements.
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Submitted on : Friday, March 13, 2015 - 8:21:56 AM
Last modification on : Thursday, June 9, 2022 - 8:18:02 AM


  • HAL Id : hal-01131129, version 1
  • PUBMED : 25288451



Manuel Blanc, Theresa L Coetzer, Martin Blackledge, Michael Haertlein, Edward P Mitchell, et al.. Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum.. BBA - Biochimica et Biophysica Acta, Elsevier, 2014, 1844 (12), pp.2306-2314. ⟨hal-01131129⟩



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