Fig. 1: Characterisation of mAb binding to the RCR-complex. | Nature Communications

Fig. 1: Characterisation of mAb binding to the RCR-complex.

From: Development of an improved blood-stage malaria vaccine targeting the essential RH5-CyRPA-RIPR invasion complex

Fig. 1

A Size exclusion chromatograms demonstrating RCR-complex formation between RH5, CyRPA and RIPR, and (B) demonstrating binary complex formation between RH5+CyRPA, and RIPR+CyRPA. C Non-reducing SDS-PAGE gel assessing binary and ternary complex formation. Coloured asterisks on chromatograms indicate which gel lanes correspond to the peaks in panels (A) and (B). Representative example of three independent experiments shown. D Size exclusion chromatogram showing a representative example of complex formation analysis between the RCR-complex and anti-RH5 mAb R5.016 [Type I, GIA-positive], and (E) anti-RH5 mAb R5.002 [Type II, GIA-negative]. F Non-reducing SDS-PAGE gel of co-immunoprecipitation of the pre-formed recombinant RCR-complex without (-) or with (+) mAb R5.016 [Type I, GIA-positive] or (G) mAb R5.002 [Type II, GIA-negative] bound to protein G agarose beads. Representative examples are shown. A representative example of two independent experiments is shown. H Bar chart summarising the number of Type I and Type II mAbs for each antigen and whether these mAbs show GIA. Source data are provided as a Source Data file.

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