Skip to main content
. Author manuscript; available in PMC: 2015 Apr 13.
Published in final edited form as: Nature. 2014 Mar 2;509(7498):55–62. doi: 10.1038/nature13036

Extended Data Figure 3. CAP256-VRC26 antibodies recognize a quaternary epitope.

Extended Data Figure 3

a, All 12 CAP256-VRC26 mAbs were tested by ELISA against gp120 from ZM53 and CAP210. Positive control antibody PG9 bound to both gp120s (not shown). b, 23 proteins and scaffolded V1V2 constructs were tested by ELISA for binding of CAP256-VRC26.03 and CAP256-VRC26.08. PG9 bound to several of these (not shown). Similar data were observed for CAP256-VRC26.06, .07 and .09. c, Binding of CAP256-VRC26.03 and CAP256-VRC26.08 to virus-like particles (VLP). VLP expressing ZM53, ZM53.K169E, CAP210, or no Env were concentrated by pelleting and used to coat ELISA plates; assays were performed without detergent to preserve the trimer spikes. Similar data were observed for CAP256-VRC26.06, .07 and .09.