Fig. 4: Parity-dependent reactivity of VAR2CSA recombinants from M200101 that bind to CSA. | Communications Biology

Fig. 4: Parity-dependent reactivity of VAR2CSA recombinants from M200101 that bind to CSA.

From: Placental malaria vaccine candidate antigen VAR2CSA displays atypical domain architecture in some Plasmodium falciparum strains

Fig. 4

a VAR2CSA recombinants expressed in Expi293 cells were analyzed in SDS-PAGE gels. Ten micrograms of purified DBL7ɛM200101 VAR2CSA (lane 2) was loaded on a 4–12% bis-tris gel and Coomassie stained. One microgram of purified full-length M200101 DBL1x-7ɛ (lane 5) and NF54 DBL1x-6ɛ (lane 4) were loaded on a 3–8% tris-acetate gel and Coomassie stained. Lane 1 and 3 are molecular weight markers (kDa). b Serial dilution of recombinant full-length VAR2CSA from M200101 (VAR2CSAM200101) and NF54 (VAR2CSANF54), DBL7ɛM200101, as well as MSP1 binding to Decorin (CSPG) was analyzed by ELISA. For each protein OD values from three biological replicates (n = 3) and a nonlinear regression curve fitting model were plotted. c Plasma pools from malaria-exposed multigravidae (red bar), primigravidae (blue bar) and children (green bar) in Mali were evaluated for antibody reactivity to VAR2CSAM200101 and DBL7ɛM200101. Full-length VAR2CSANF54 and DBL5ɛFCR3 proteins were used as comparator antigens. OD values from three independent assays (n = 3) are shown as mean ± SD.

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