Fig. 3: Conservation of GSH-binding pocket in enteroviruses.

a Multiple sequence alignment of the VP1 and b VP3 subunit sequences of PV3-SC8 with several major enteroviruses. Amino acid residues that form the GSH-binding site are marked with circles above the sequence and coloured blue (VP1 protomer A), grey (VP1 protomer B) and red (VP3 protomer A). Enterovirus species A, B, C, D, F and rhinovirus A and B are marked alongside the alignments. c, d Electrostatic charges (±5 kT e⁻¹) mapped onto the molecular surface of c PV3-SC8^GPP3+GSH and d the EVF3 GSH complex and coloured from blue (positive charge) to red (negative charge). e Phylogenetic tree derived from a structure-based alignment of the representative set of major enteroviruses aligned in a. Those reported to be dependent/stabilised by GSH are marked: T where this was reported in reference ²⁶, D where reported in reference ³⁰ and B where reported in this paper. Abbreviations for each branch of the tree (PDB ID): CVA16 coxsackievirus A16 (5C4W), EVA71 enterovirus A71 (3VBH), CVB3 coxsackievirus B3 (6ZCL), CVB4 coxsackievirus B4 (6ZCK), CVA9 coxsackievirus A9 (1D4M), ECV1 echovirus 1 (1EV1), ECV7 echovirus 7 (2 × 51), ECV11 echovirus 11 (1H8T), PV1 poliovirus type 1 Mahoney (1HXS), PV2 poliovirus type 2 Lansing (1EAH), PV3 poliovirus type 3 Sabin (1PVC), PV3-SC8^GPP3+GSH poliovirus type 3 Saukett in complex with GPP3 and GSH (8AYX), EVD68 enterovirus D68 (4WM8), EVF3 enterovirus F3 (6T4C), HRVA16 human rhinovirus 16 (1AYM), HRVB14 human rhinovirus 16 (4RHV).