Cryo-EM structure of N751-2C06.01 in complex with BG505 DS-SOSIP reveals antibody recognition at the fusion-peptide site of vulnerability
(A) Cartoon representation of 2C06 in complex with BG505 DS-SOSIP. 2C06 bound at the fusion-peptide site and interacted with fusion peptide (FP), shown in red. Antibody heavy chain (H) is shown in blue, light chain (L) in pale cyan, gp41 in dark gray, and gp120 in light gray.(B) Density map for fusion peptide N-terminal residues. The structure is shown in cartoon representation, with fusion peptide and antibody side chains interacting with fusion peptide shown in sticks. Color codes are as in (A).(C) 2C06 epitope details. Env trimer is shown as surface with subunits in different shades of gray and the epitope surface in magenta. Antibody CDRs and FRs involved in binding are shown in cartoon representation, with interacting side chains shown in sticks. The glycan hole at S241 is on the edge of the epitope and is labeled.(D) Overall sequence variation of HIV-1 group M Env glycoproteins. Normalized sequence entropy is mapped on the trimer surface, with absolutely conserved residues (entropy of 0) in white and the most diverse residues (entropy of 1) in purple.(E) HIV-1 Env sequence variation around the 2C06 epitope. 2C06 epitope is shown as a blue outline. Part of the 2C06 epitope is highly variable (labeled). The residue at 241 is well conserved with over 96% of isolates having an See also 