α2-Macroglobulin Can Crosslink Multiple Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Molecules and May Facilitate Adhesion of Parasitized Erythrocytes
Fig 2
Binding of native and MA-activated α2M to HB3VAR06.
(A) Titration of binding of native α2M (black circles) and α2M-MA (white circles) to recombinant full-length HB3VAR06 measured by ELISA. Means and SD are indicated. (B) Titration of binding of native α2M (black circles) and α2M-MA (white circles) to HB3VAR06+ IEs measured by flow cytometry. Means and SD are indicated. (C) Activation of α2M measured by SDS gel electrophoresis of soluble and immobilized α2M in the presence of mPEG: soluble α2M alone (lane 1), soluble α2M and MA (lane 2), soluble α2M and FV6 (lane 3), bead-immobilized α2M-FV6 complexes alone (lane 4), and bead-immobilized α2M-FV6 complexes and MA (lane 5). While native α2M was detectable in all lanes, activated α2M having a higher molecular weight than native α2M due to incorporation of mPEG was only detected in the presence of MA (lanes 2 and 5).