Cryo-EM Structure of a Novel Calicivirus, Tulane Virus
Open accessAbstract
Tulane virus (TV) is a newly isolated cultivatable calicivirus that infects juvenile rhesus macaques. Here we report a 6.3 Å resolution cryo-electron microscopy structure of the TV virion. The TV virion is about 400 Å in diameter and consists of a T = 3 icosahedral protein capsid enclosing the RNA genome. 180 copies of the major capsid protein VP1 (∼57 KDa) are organized into two types of dimers A/B and C/C and form a thin, smooth shell studded with 90 dimeric protrusions. The overall capsid organization and the capsid protein fold of TV closely resemble that of other caliciviruses, especially of human Norwalk virus, the prototype human norovirus. These close structural similarities support TV as an attractive surrogate for the non-cultivatable human noroviruses. The most distinctive feature of TV is that its C/C dimers are in a highly flexible conformation with significantly reduced interactions between the shell (S) domain and the protruding (P) domain of VP1. A comparative structural analysis indicated that the P domains of TV C/C dimers were much more flexible than those of other caliciviruses. These observations, combined with previous studies on other caliciviruses, led us to hypothesize that the enhanced flexibility of C/C dimer P domains are likely required for efficient calicivirus-host cell interactions and the consequent uncoating and genome release. Residues in the S-P1 hinge between the S and P domain may play a critical role in the flexibility of P domains of C/C dimers.
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The P2 domains of FCV form a rhombus-shaped structure with a flatter outer surface, similar to that of SMSV and Tulane virus.
“Conversely, the P2 domains of FCV form a rhombus-shaped structure with a flatter outer surface (similar to that of SMSV and Tulane virus [36, 37]).”
From Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures (2017) · cites this paper as [37]
The Results section (“The Fold of the Major Capsid Protein (VP1) of TV”; page unavailable) compares Tulane virus’s P2 subdomain with SMSV but does not describe a rhombus shape or a flatter outer surface. The Results section on flexible P domains also compares Tulane virus and FCV without making that shape claim. Searches for “rhombus” and for FCV, SMSV, and P2 surface shape found no passage that verifies the attributed comparison. (LLM, conf=0.73)
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- Authors
- Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., & Jiang, W.
- Affiliations
- Purdue University West Lafayette (US)
- Cincinnati Children's Hospital Medical Center (US)
- Corresponding author
- Jiang, Wen
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-03-22
- Volume
- 8
- Issue
- 3
- Pages
- e59817
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3606144
- OpenAlex
- W1992113841
- Cited by
- 34
- References
- 41
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 3 · 2020: 3 · 2019: 2 · 2017: 2 · 2016: 7 · 2015: 3 · 2014: 5 · 2013: 2
- FWCI
- 4.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Purdue e-Pubs (Purdue University System) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Agriculture
- Purdue University
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI037093, R01AI089634)
- National Center for Research Resources (S10RR023011)
- 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
- Tulane virus, calicivirus, norovirus, VP1 major capsid protein, icosahedral capsid, protruding domain, host-virus interaction, genome release
- MeSH terms
- Caliciviridae, Cryoelectron Microscopy, Capsid Proteins
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