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Fig. 2 | Malaria Journal

Fig. 2

From: Strain-transcending neutralization of malaria parasite by antibodies against Plasmodium falciparum enolase

Fig. 2

Antigenic specificity of mAb H12E1. a Sequences of pentapeptide insert in different variants. b ELISA of mAb binding to different variants of rPfeno. Oligomeric state of WT and S108G-rPfeno was dimeric while ∆5-rPfeno, W105, 107K-rPfeno and W105, 107A-rPfeno were in the monomeric form. 15 ng of purified protein of each variant form was coated on the plates. c ELISA of mAb binding to GST-tagged forms of rPfeno variants. In GST-tagged forms, all variants of rPfeno formed dimers (or higher oligomers). Wells were coated with 5 ng of purified protein of each variant. Variation in insert sequence affected the mAb binding while oligomeric state (monomer or dimer Pfeno) did not have any effect on reactivity. d Competitive ELISA with EWGWS containing peptide led to displacement of H12E1 from rPfeno. Peptide concentration was varied from 0-100 µM. e Titration with an irrelevant peptide epitope resulted in no displacement of the mAb by the irrelevant peptide. f Reactivity of various mAbs with WT-NPs and Rec-NPs. mAb directed against EWGWS i.e. H12E1 showed strong reactivity to the EWGWS containing Rec-NPs (incorporated with a clone peptide sequence ASKNEWGWSKSKS) as compared to WT-NPs

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