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. Author manuscript; available in PMC: 2013 Sep 27.
Published in final edited form as: J Mol Biol. 2012 Nov 15;425(2):444–456. doi: 10.1016/j.jmb.2012.11.010

Figure 1.

Figure 1

Yeast display of gp120. (a) Homology model of stripped core showing the inner domain (white), outer domain (blue), the short glycosylated peptides that have replaced the V1/V2 loop (orange), V3 loop (red), and bridging sheet (purple), and the VRC01 contact residues (yellow). Beneath it, a schematic of yeast display vector pCHA showing gp120, the C-terminal Aga2 fusion partner, and two epitope tags. (b) Representative flow cytometry dot-plot of yeast displaying stripped core gp120, bound to both an anti-CMyc antibody (x axis) and the broadly neutralizing antibody VRC01 (y axis). (c) Binding isotherms of yeast-displayed stripped core gp120 to a panel of CD4 binding site-directed antibodies. Equilibrium KD values for the antibodies are as follows: VRC01, 0.8 nM; PGV04, 0.9 nM; b12, 41 pM; b6, 24 pM; b13, 0.9 nM; CD4-Fc, 5.6 nM. (d) Binding of secreted stripped core gp120 to yeast displaying the scFv of antibody VRC01. Equilibrium KD values for the interactions are: Stripped Core, 8.7 nM; Fc Stripped Core, 1.1 nM.