Fig. 4

Involvement of V1 length in resistance to bNAbs PGT135, b12 and 12A21. Correlation plots between the V1 length and neutralization sensitivity for mAbs PGT135 (a), PGT121 (b), b12 (c), 12A21 (d), and VRC01 (e). The r and p values for the linear regression are given. For correlations that were statistically significant, the regression line is shown. (f) Top view of the Env trimer with one protomer shown in dark blue and the other protomers in light blue. The V1 loops are indicated in red and the N332-glycan is shown on one protomer. g View of the trimer in the same orientations as f in complex with PGT135 (yellow) and PGT122 (gray). We used PGT122 in our figure instead of PGT121 since the HIV-1 Env trimer structures were solved in complex with PGT122, whereas for PGT121 the structure was only solved in complex with a glycan [42] or recently a complex of a PGT121 precursor in complex with the HIV-1 Env trimer [120]. It was shown that PGT121 and PGT122 bind to the Env protein with the same angle of approach in a very similar way. h Detailed view of the expected clash of PGT135 with the V1 loop indicated by an asterisk. i View of the trimer in the same orientations as f in complex with b12 (green) and 12A21 (dark green) and VRC01 (gray). j Detailed view of the expected clash of b12 with the V1 loop indicated by an asterisk. The figures were drawn using pymol (www.pymol.org) by aligning the gp120 structures of 4JM2.pdb (gp120 plus PGT135; PMC3823233 [60]), 2NY7.pdb (gp120 plus b12: PMC2584968 [121]), 4JPW.pdb (gp120 plus 12A21; PMC3792590 [122]), and 3NGB.pdb (gp120 plus VRC01; PMC2981354 [123]) with the dark blue protomer of the BG505 SOSIP.664 trimer in complex with PGT122 and 35O22 (4TVP.pdb [43])