Fig. 3: RON2L is bound to AMA1 in the designed immunogens, preventing accessibility to the RON2L binding site.
From: Structure-based design of a strain transcending AMA1-RON2L malaria vaccine
a Representative biolayer interferometry (BLI) traces used to quantitatively measure the binding of immunogens to IgNAR 14I-1 demonstrating inaccessibility of the epitope located in the RON2L binding pocket in the immunogens. Immunogens were two-fold serially diluted in the range of 200 nM to 3.125 nM. b IgNAR 14I-1 shows little or no binding to immunogens in three independent ELISAs. c Representative BLI traces used to measure the binding of immunogens to exogenous RON2L demonstrating that the binding site for exogenous RON2L is occupied by the fused RON2L in the designed immunogens. Immunogens were two-fold serially diluted in the range of 200 nM to 3.125 nM. d Exogenous RON2L does not bind to immunogens in three independent ELISAs. In b and d, bovine serum albumin (BSA) was used as a negative control. Source data are provided as a Source data file.
