Regular ArticlePlasmodium falciparum:Structural and Functional Domains of the Mature-Parasite-Infected Erythrocyte Surface Antigen☆,☆☆
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Cited by (14)
Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton
2010, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :The presence of binding sequences encoded in -F19b however, cannot be ruled out because despite numerous attempts of optimise the yield of -F19b full length fusion protein, the relative quality of the -F19b used was poor when compared to that of -F19, F19a and -F19c (Fig. 3B). Residues adjacent to defined binding regions that also contribute to overall interactions between RBC membrane skeleton and parasite proteins have been previously described for other P. falciparum proteins, including MESA and PfEMP3 [15,38]. Additionally, since comparatively more of the input -F19a protein remained in the insoluble fraction than -F19c (Fig. 3C), it is possible that -F19a may possess higher affinity for its binding partner in the RBC membrane skeleton than -F19c, but further experimentation would be required to confirm this suggestion.
Plasmodium falciparum: Genetic and immunogenic characterisation of the rhoptry neck protein PfRON4
2009, Experimental ParasitologyInteractions of Plasmodium falciparum erythrocyte membrane protein 3 with the red blood cell membrane skeleton
2007, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Interestingly, the same phenomenon was observed in the actin co-sedimentation assays (Fig. 6C), where residues downstream of the 14-residue region appeared to increase the intensity of the interaction. Such enhancement of interactions by adjacent residues has previously been reported in the binding of the parasite protein MESA to its binding partner protein 4.1R [36]. The observation that the PfEMP3–membrane skeleton interaction occurs in vitro to IOVs, where the supramolecular structure of the spectrin-actin network and the conformation of the individual proteins is conserved, as well as in vivo provides confidence that this is a physiologically relevant interaction.
Characterisation of a Tryptophan-rich Plasmodium falciparum antigen associated with merozoites
2004, Molecular and Biochemical ParasitologyCommon trafficking pathway for variant antigens destined for the surface of the Plasmodium falciparum-infected erythrocyte
2004, Molecular and Biochemical ParasitologyMature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells
2003, BloodCitation Excerpt :Here, using recombinant 4.1R and MESA proteins, we mapped the region of 4.1R that binds the 19-residue region of MESA and also demonstrated competition between MESA and p55 for 4.1. Fragments of 4.1R and MESA were amplified by polymerase chain reaction (PCR) as previously described5 (Figure 1), either from cDNAs of 4.1R8 or appropriate genomic DNA subfragments of the MESA gene.3,7 The resulting fragments were cloned into the Escherichia coli protein expression plasmids pGEX-KG10 or pET-31b(+) (Novagen, Darmstadt, Germany), and glutathione S-transferase (GST)– and histidine-tagged fusion proteins were expressed and purified using standard affinity chromatography under native purification conditions.3,8,11
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We thank Jutta Kun and Fiona Smith for expert technical assistance. J.F.J.K. was supported by a fellowship of the Deutsche Forschungsgemeinschaft. K.J.W. is the recipient of a Monash University Graduate Scholarship. This work is supported by Grant DK 32094 from the National Institutes of Health and the Australian National Health and Medical Research Council.
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The sequence data have been submitted to GenBank and assigned the Accession No. AF056936.
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