High-Resolution Cryo-Electron Microscopy Structures of Murine Norovirus 1 and Rabbit Hemorrhagic Disease Virus Reveal Marked Flexibility in the Receptor Binding Domains
Open accessAbstract
Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the three-dimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to ∼8-Å resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.
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The P domains of vesivirus 2117, sapovirus and FCV appear to be raised off the S domain, as previously observed for RHDV and MuNV-1, in contrast to the P domains of NoV, which form a more collapsed conformation.
“The P domains of vesivirus 2117, sapovirus and FCV appear to be raised off the S domain, as previously observed for RHDV and MuNV-1, in contrast to the P domains of NoV, which form a more collapsed conformation in relation to the S domain [33, 34].”
From Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures (2017) · cites this paper as [34]
MuNV exhibits prominent horn-like protrusions on the outer surface of the P2 domain of VP1.
“MuNV also exhibits prominent horn-like protrusions on the outer surface of the P2 domain of VP1 [34].”
From Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures (2017) · cites this paper as [34]
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Research works printed but not linked: 1
- [1]1. Chen, R., J. D. Neill, M. K. Estes, and B. V. V. Prasad. 2006. X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. U. S. A. 103: 8048-8053.
Cited by
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Cryo-EM Structure of a Novel Calicivirus, Tulane Virus
Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., & Jiang, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059817 · Cited by 34 · see citing works
Conley, M., Emmott, E., Orton, R., Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S., & Bhella, D. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000658 · Cited by 8 · see citing works
- Authors
- Katpally, U., Voss, N. R., Cavazza, T., Taube, S., Rubin, J. R., Young, V. L., Stuckey, J., Ward, V. K., Virgin, H. W., Wobus, C. E., & Smith, T. J.
- Affiliations
- Donald Danforth Plant Science Center (US)
- Scripps Research Institute (US)
- University of Michigan (US)
- University of Otago (NZ)
- Washington University in St. Louis (US)
- ORCID
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2010-06
- Volume
- 84
- Issue
- 11
- Pages
- 5836-5841
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC2876586
- OpenAlex
- W2014673399
- Cited by
- 77
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 5 · 2019: 5 · 2018: 4 · 2017: 3 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 9 · 2012: 8
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI065982, AI054483-07, R01AI054483, R01AI080611, U54AI057153, AI080611, AI065982-04)
- National Center for Research Resources (P41RR017573, RR 17573)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Viral gastroenteritis research and epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- murine norovirus 1, rabbit hemorrhagic disease virus, virus-like particles, 3D reconstruction
- MeSH terms
- Animals, Binding Sites, Protein Conformation, Rabbits, Receptors, Virus, Hemorrhagic Disease Virus, Rabbit, Pliability, Cryoelectron Microscopy, Imaging, Three-Dimensional, Norovirus, Mice
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