Antivirals blocking entry of enteroviruses and therapeutic potential

Fig. 1. Enterovirus capsid organization and features. a Overall view of the enterovirus capsid comprising the VP1 (red), VP2 (blue) and VP3 (yellow). PDB ID: 4RQP [8]. The green lines indicate the boundaries of one pentamer. The black lines indicate the icosahedral symmetric subunit. The five, three, twofold symmetry axes are labeled and highlighted in grey. The cyan lines separate VP1 (red), VP2 (blue) and VP3 (yellow). Black arrows indicate the canyon region and the fivefold axis region formed by five VP1. b Canonical enterovirus protomer formed by VP1 (red), VP2 (blue), VP3 (yellow) and VP4 (green). PDB ID: 6GZV [9]. The canyon is highlighted in grey transparent and is indicated by a black arrow. Antiviral compounds that bind to the two binding pockets which are VP1 hydrophobic pocket and VP1–VP3 interprotomer pocket are shown in cyan and magenta, respectively

Fig. 2. The structure of poliovirus in complex with PVR (PDB ID: 3EPD) [94]. a Overall view of the canonical picornavirus protomer with the capsid proteins VP1, VP2, VP3 and VP4 are shown in red, yellow, blue and green, respectively. The apical domain of PVR that binds to the canyon of the protomer is shown magenta. b The amino acids that make contacts with the canyon are shown in sticks and labeled

Fig. 3. Three-dimensional structure of EV-A71 in complex with SCARB2 (PDB: 6I2K) [18]. The EV-A71 capsid proteins VP1, VP2, VP3 and VP4 are shown in red, yellow, blue and green, respectively. The receptor SCARB2 is shown in cyan. VP2 EF loop and VP1 GH loop of EV-A71 interact with α5 and α7 helices of SCARB2 to form the interface of the complex