Figure 5
Consensus sequence alignment and location of the epitope on a parechovirus capsid. (a) Top-down surface view of PeV-1 structure (PDB: 4z92) asymmetric unit consisting of VP0 (blue), VP1 (magenta), and VP3 (grey) proteins. The core of the putative epitope is colored in green, while the residues of the conserved flanking regions that exhibit surface exposure are colored in orange. Structurally the epitope is located near the junction of the three capsid proteins, which is also structurally close to the RGD motif in VP1, known to be important for integrin binding. The highly conserved flanking regions of the epitope are likely important in stabilizing the base structure of the epitope, which itself has a higher degree of flexibility. (b) Sequence alignment of the VP0 residue range obtained from Pepscan’s CLIPS analysis for PeV-1–6 with residues numbered based on the PeV-A1 (Harris) prototype sequence (acc. no. L02971). The area boxed in red represents residues with surface exposure. The flanking regions of the core, VVTYDSKL, are seen highly conserved across different PeV type, while the core alignment itself shows higher flexibility.
