Comparison to HRV-2 ( Figure 3D ) also revealed the impact of VP1 deletions. The resulting loops were shorter, which ablated any analogue of antigenic site A and may hamper binding of the VLDL-R molecule, the only LDLR family member with a welldefined footprint. The area in VP1 forming site B was altered due to the presence of more hydrophilic amino acids at the equivalent positions in HRV-QPM ( Figure 3D ; VP1 site B, arrow). Deletions were apparent but did not confer obvious structural changes to the VP2 portion of site B. Furthermore, in antigenic site C (VP2), a single deletion and a hydrophobic to hydrophilic amino acid change contributed to a protrusion in HRV-QPM compared to the same region in HRV-2.