Fig. 4: Comparison of HA fusion subdomain-interacted domains of VH and VL from AF4H1K1 and FI6v3. | Cell Discovery

Fig. 4: Comparison of HA fusion subdomain-interacted domains of VH and VL from AF4H1K1 and FI6v3.

From: Light chain modulates heavy chain conformation to change protection profile of monoclonal antibodies against influenza A viruses

Fig. 4: Comparison of HA fusion subdomain-interacted domains of VH and VL from AF4H1K1 and FI6v3.

a Structural overlapping between AF4H1K1/H3 complex and FI6v3/H3 complex (PDB ID, 3ZTJ). AF4H1K1 VH is in light pink and the FI6v3 VH is labeled with green. H3 HA binding to AF4H1K1 is present in cyan and H3, which is in complex with FI6v3, is in white. Red arrows suggest the lift up of AF4H1K1 key components toward HA compared with FI6v3. b Interaction of FI6v3 VL with two H3 HA protomers (PDB ID, 3ZTJ). The structure is in surface presentation, with one protomer in white color and the other in green. FI6v3 LCDR3 (purple) reaches out to the fusion peptide of the neighboring HA protomer and forms two hydrogen bonds between LCDR3 Asn28, Tyr29 and neighboring HA1 Arg321, HA2 Ile10. Labels for FI6v3 LCDR are in purple and the others of HA are in black. c Structural overlapping between AF4H1K1/H3 complex and FI6v3/H3 complex (3ZTJ) in the light chain–HA interface. AF4H1K1 light chain LCDR1 loop (yellow) interacts with two amino acid residues at HA2 stalk (cyan): one is Gln42 and the other is Asp46. There is no direct interaction between AF4H1K1 light-chain LCDR3 loop and HA (cyan), whereas both LCDR1 and LCDR3 loops of FI6v3 light chain are involved in the interaction with HA fusion subdomain (white). FI6v3 LCDR1 shows weak attachment to HA2. In addition, FI6v3 LCDR3 reaches out to the fusion peptide of the neighboring HA in FI6v3/H3 complex

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