Equine Rhinitis A Virus and Its Low pH Empty Particle: Clues Towards an Aphthovirus Entry Mechanism?
Figure 3
(A) A phylogenetic tree [20] based on a structural alignment of complete protomers (VP1,2,3 & 4) for picornaviruses (RCSB protein data bank code (Berman et al. 2000)): Theiler's virus (1TME), Mengo virus 1 (1MEC), Mengo virus 2 (2MEV) FMDV A10 (1QBE), FMDV O (1BBT), FMDV reduced (1FOD), HRV 14 (4RHV), HRV 16 (1ND2), HRV 1A (1R1A), Swine vesicular disease virus (1OOP), Coxsackie virus 9 (1D4M), Echovirus 1 (1EV1), PV 2 (1EAH). (B) Surface depictions of FMDV (1FOD), ERAV and Mengovirus (2MEV) coloured by radial height (with the same colour scheme for all three particles) to illuminate surface features [55]. (C) 5-fold pores. FMDV, ERAV and PV 1 Mahoney (1HXS) are shown, above as slices through icosahedral 5-fold axes (the axes are vertical), below looking down the pore. In each set of representations the view-point and scale is the same for all three viruses. (D) Capsid porosity measured by the accessibility of viral RNA within the capsid to an RNA binding fluorescent dye at 25°C and after thermal uncoating by incubation at 60°C for ERAV and PV 1 Mahoney.