The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry
Open accessAbstract
SUMMARY To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. Here, using single-particle cryo-electron microscopy, we report a 3.3 Å structure of the primed, infectious subvirion particle of aquareovirus. The density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. Our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that Lys84 and Glu76 may facilitate this autocleavage in a nucleophilic attack. We observe a myristoyl group, covalently linked to the N terminus of the penetration protein and embedded in a hydrophobic pocket. These results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger.
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Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
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Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
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EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
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Henderson, R., Sali, A., Baker, M. L., Carragher, B., Devkota, B., Downing, K. H., Egelman, E. H., Feng, Z., Frank, J., Grigorieff, N., et al. (2012) · Structure · doi:10.1016/j.str.2011.12.014 · Cited by 505
Cryo-electron microscopy--a primer for the non-microscopist
Milne, J. L. S., Borgnia, M. J., Bartesaghi, A., Tran, E. E. H., Earl, L. A., Schauder, D. M., Lengyel, J., Pierson, J., Patwardhan, A., & Subramaniam, S. (2013) · The FEBS Journal · doi:10.1111/febs.12078 · Cited by 277
Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu
Ho, C.-M., Li, X., Lai, M., Terwilliger, T. C., Beck, J. R., Wohlschlegel, J., Goldberg, D. E., Fitzpatrick, A. W. P., & Zhou, Z. H. (2020) · Nature Methods · doi:10.1038/s41592-019-0637-y · Cited by 115
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Metadata
- Authors
- Zhang, X., Jin, L., Fang, Q., Hui, W. H., & Zhou, Z. H.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 141
- Issue
- 3
- Pages
- 472-482
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2117756276
- Cited by
- 319
- References
- 5
- FWCI
- 24.73
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zhang, X., Jin, L., Fang, Q., Hui, W. H., & Zhou, Z. H. (2010). 3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry. Cell. https://doi.org/10.1016/j.cell.2010.03.041
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