Figure 4.

NPC1-C Mimics Similar but Stronger Interactions like the Glycan Cap in the Unprimed GP

(A) In the unprimed GP structure, the glycan cap utilizes two aromatic residues, F225 and Y232, to insert into the hydrophobic receptor binding cavity in the head of GPcl.

(B) NPC1-C takes advantage of four aromatic residues (Y423, F503, F504, and Y506) and one hydrophobic residue P424 to interact with the hydrophobic cavity. In particular, the residue F503 inserts into the cavity at a deeper position. Thus, the binding of NPC1-C mimics the interaction like the glycan cap but likely with a better binding capacity by providing more aromatic residues.

(C) An MARV-neutralizing antibody MR79 targets the hydrophobic binding cavity of MARV GP through aromatic residues (F111.2 and Y112.2).