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Figure 4 | Virology Journal

Figure 4

From: Identification of broadly neutralizing antibody epitopes in the HIV-1 envelope glycoprotein using evolutionary models

Figure 4

Three-dimensional predictions for CAP255. (A) Amino acid residues that were weakly (2 ≤ B k  < 4), moderately (4 ≤ B k  < 6) and strongly (B k  ≥ 6) associated with ID50 titer using the ConC reference sequence are shown with light, intermediate and dark green, respectively. There is evidence for a cluster of sites with moderately large Bayes factors on the three-dimensional surface, as might be expected of a B cell epitope. (B) Posterior probabilities of a conformational epitope using the three-dimensional Metropolis algorithm. The surface of the protein (PDB ID: 2B4C) was shaded from dark blue (posterior probability = 0) to red (posterior probability = 1) according to the posterior probability assigned to each amino acid residue. There was evidence for a conformational epitope involving the C3 region (residues in the light blue region have posterior probabilities of approximately 0.2).

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