Fig. 6. Epitope mapping of C12G6.

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Fig. 6. Epitope mapping of C12G6. Epitope mapping of C12G6. (A) Amino acid substitutions found in the HA of C12G6-induced escape mutants. (B) Surface representation illustration and conservation analysis of the neutralizing epitope recognized by C12G6 on the HA trimer model of B/Brisbane/60/2008 (Protein Data Bank code: 4FQM) using the DS Visualizer 1.7. The epitope was determined using a molecular docking strategy. One HA protomer of the HA trimer is colored in cyan, whereas the other two protomers are colored in gray. The residues are colored according to the conservation of contact residues across all available influenza B virus sequences: green, more than 98% conserved; yellow, 75 to 98% conserved. Residue numbers are shown, with RBS residues in red and others in black. (C) Reactivity of C12G6 with WT or mutant BR/2008 HAs expressed in HEK293T cells. The mean fluorescence intensities (MFIs) from flow cytometry profiles are shown. Mock, mock-transfected cells. *P < 0.05, compared to the WT group. Statistical analysis was performed by t test. (D) Illustration of the identified key C12G6 epitope residues, colored in red, with the RBS domain colored in blue. The residue numbers with amino acid substitutions found in the C12G6 escape mutants are shown in red, and others are shown in black. (E) Comparison of C12G6 and CR8033 contact residues on influenza B HA. Brown, contact residues unique to C12G6; blue, contact residues unique to CR8033; light yellow, common contact residues of both antibodies. The residue numbers are shown, with RBS residues in red and others in black. (F) Comparison of epitopes of C12G6 and two representative bnAbs (CR8033-like and CR9114-like antibodies) using a competition ELISA test. C12G6 was used as a competitor, and C5G6 was used as a negative control. *P < 0.05, compared to the control group. Chenguang Shen et al., Sci Transl Med 2017;9:eaam5752 Published by AAAS