Fig. 4

Pfs38 binds human erythrocytes via Glycophorin A and is required for invasion of red blood cells. a Recombinant Pfs38, Pfs12 and Pfs41 were incubated with uninfected human erythrocytes and bound proteins were eluted from the erythrocytes after centrifugation through oil. PvRII was used as a positive control for erythrocyte binding assay, while an internal protein ClpQ was used as a negative control for the assay; b Erythrocyte binding assay of recombinant Pfs38 with untreated (UN) and neuraminidase treated (NM) RBCs. c Glycophorin A is the erythrocyte receptor through which Pfs38 binds human erythrocytes. ELISA binding assay was performed to study the interaction between Glycophorin A and recombinant Pfs38. As a control, GLURPR2 and PfMLH protein were used. Error bars indicate mean ± SEM of duplicate measurements; d A model of Pfs38 protein complex based on protein–protein interactions and protein-erythrocyte interaction; e Invasion inhibition assay was performed on schizont stage using α-Pfs38 purified IgG at concentration of 2, 5 and 10 mg/mL and percent inhibition was calculated. Bars indicate mean ± SEM of duplicate measurements