Fig. 3: Structural basis for improved stability with intact functional antigenicity. | Nature Communications

Fig. 3: Structural basis for improved stability with intact functional antigenicity.

From: A stabilized tandem antigen chimera that elicits potent malaria transmission-reducing activity

Fig. 3: Structural basis for improved stability with intact functional antigenicity.

a STAC bound by Fabs LMIV230-01, RUPA-97, TB31F, and RUPA-44 determined by cryo-EM. b STAC structure overlayed with individual Pfs230-D1 and Pfs48/45-D3 domains with Cα RMSD values plotted for each alignment (PDB 9N8N and 7UXL). c All mutations involved in stabilization of STAC. The Pfs230 N585Q mutation to ablate a potential N-glycosylation site is omitted for clarity. d–k Cryo-EM structure of STAC overlayed with previous antigen-bound antibody structures and antibody Cα RMSD values plotted for each alignment (PDBs 7UVQ, 7JUM, 6E63, and 7UXL). Gray coloring indicates previously reported structures when overlayed for comparison. CDR residues (Kabat boundaries) are indicated with shading.

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