6CSG
CryoEM structure of human enterovirus D68 full native virion
Summary for 6CSG
| Entry DOI | 10.2210/pdb6csg/pdb |
| EMDB information | 7567 7569 7571 7572 7583 7589 7592 7593 7598 7599 7600 |
| Descriptor | viral protein 1, viral protein 3, viral protein 2, ... (5 entities in total) |
| Functional Keywords | virus, genome release, acid |
| Biological source | Enterovirus D68 More |
| Total number of polymer chains | 4 |
| Total formula weight | 94937.22 |
| Authors | Liu, Y.,Rossmann, M.G. (deposition date: 2018-03-20, release date: 2018-12-19, Last modification date: 2024-03-13) |
| Primary citation | Liu, Y.,Sheng, J.,van Vliet, A.L.W.,Buda, G.,van Kuppeveld, F.J.M.,Rossmann, M.G. Molecular basis for the acid-initiated uncoating of human enterovirus D68. Proc. Natl. Acad. Sci. U.S.A., 115:E12209-E12217, 2018 Cited by PubMed Abstract: Enterovirus D68 (EV-D68) belongs to a group of enteroviruses that contain a single positive-sense RNA genome surrounded by an icosahedral capsid. Like common cold viruses, EV-D68 mainly causes respiratory infections and is acid-labile. The molecular mechanism by which the acid-sensitive EV-D68 virions uncoat and deliver their genome into a host cell is unknown. Using cryoelectron microscopy (cryo-EM), we have determined the structures of the full native virion and an uncoating intermediate [the A (altered) particle] of EV-D68 at 2.2- and 2.7-Å resolution, respectively. These structures showed that acid treatment of EV-D68 leads to particle expansion, externalization of the viral protein VP1 N termini from the capsid interior, and formation of pores around the icosahedral twofold axes through which the viral RNA can exit. Moreover, because of the low stability of EV-D68, cryo-EM analyses of a mixed population of particles at neutral pH and following acid treatment demonstrated the involvement of multiple structural intermediates during virus uncoating. Among these, a previously undescribed state, the expanded 1 ("E1") particle, shows a majority of internal regions (e.g., the VP1 N termini) to be ordered as in the full native virion. Thus, the E1 particle acts as an intermediate in the transition from full native virions to A particles. Together, the present work delineates the pathway of EV-D68 uncoating and provides the molecular basis for the acid lability of EV-D68 and of the related common cold viruses. PubMed: 30530701DOI: 10.1073/pnas.1803347115 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.17 Å) |
Structure validation
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