Crystal structure of human enterovirus 71

Abstract

Enterovirus 71 is a picornavirus associated with fatal neurological illness in infants and young children. Here, we report the crystal structure of enterovirus 71 and show that, unlike in other enteroviruses, the "pocket factor," a small molecule that stabilizes the virus, is partly exposed on the floor of the "canyon." Thus, the structure of antiviral compounds may require a hydrophilic head group designed to interact with residues at the entrance of the pocket.

Fig. 1

The EV71 capsid structure. (A) Cartoon diagram of EV71 icosahedral asymmetric unit showing VP1 (blue), VP2 (green), VP3 (red), VP4 (yellow) calcium ions (magenta) and the pocket factor (orange). The positions of the prominent capsid surface features are indicated by dashed lines. (B) Molecular surfaces of EV71 and Poliovirus of five icosahedral asymmetric units viewed down a fivefold axis. (C) The EV71 pocket factor electron density (green) was calculated by model-free phase extension (3). The main-chain is shown as lines connecting Cα atoms. Side-chains are displayed as stick models. (D) Positions of pocket factors in EV71 (orange), HRV1A (yellow), bovine enterovirus (green), and Poliovirus 1 (magenta). (C, D) The arrow shows the entrance to the pocket.