Fig. 3: ACS101 heavy chain interactions with the CD4bs of AMC009 SOSIP and comparison to other VH1-2 and VH1-46-derived CD4bs bNAbs. | Nature Communications

Fig. 3: ACS101 heavy chain interactions with the CD4bs of AMC009 SOSIP and comparison to other VH1-2 and VH1-46-derived CD4bs bNAbs.

From: Identification of IOMA-class neutralizing antibodies targeting the CD4-binding site on the HIV-1 envelope glycoprotein

Fig. 3

a Cryo-EM map and model of Fabs ACS101 and ACS124 in complex with AMC009 SOSIP (gp120; light brown, gp41; gray and N-linked glycans; green). ACS101 and ACS124 Fab HC and LC are color coded as indicated. Only the variable domains of Fabs ACS101 and ACS124 and one gp41-gp120 heterodimer are shown as ribbons and fitted into the cryo-EM map. ACS101 is framed by the N197, N234, N276 and N362 glycans, which are colored green in the right-hand panel. b Key interactions of ACS101, VH1-2-derived bNAbs IOMA (PDB:5T3Z) and VRC01 (PDB:3NGB), VH1-46-derived bNAb 8ANC131 (PDB:4RWY) and CD4 (PDB:1G9N) with HIV-1 gp120 (shown in light brown) at four sites: D368, F43 cavity, V5 loop and Loop D. All interactions are shown with the gp120 subunit that the bNAbs were complexed with: ACS101 (clade B AMC009 SOSIP), IOMA (clade A BG505 SOSIP), VRC01 (clade A/E 93TH057 gp120), 8ANC131 (clade B YU2 gp120) and CD4 (clade B YU2 gp120). The F43 cavity is shown as a molecular map generated at 3.5 Å resolution from the gp120 atomic coordinates with UCSF Chimera60. Expected H-bonds and salt bridges are shown as dotted lines using a cut-off distance of 3.2 Å.

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