Crystallization and preliminary crystallographic analysis of San Miguel sea lion virus: An animal calicivirus
Abstract
The Caliciviridae is a family of nonenveloped, icosahedral, positive-sense single-stranded RNA viruses. This family of viruses consists of both animal and human pathogens. Adapting human caliciviruses to cell culture has not been successful, whereas some animal caliciviruses, including San Miguel sea lion virus, have been successfully propagated in vitro. Here we report the crystallization of San Miguel sea lion virus serotype 4 (SMSV4) and the preliminary X-ray crystallographic analysis of the crystals. SMSV4 have been crystallized using the hanging-drop method. These crystals diffracted to approximately 3A resolution using a synchrotron radiation source. A single crystal under cryo-conditions yielded a complete set of diffraction data. Data processing of the diffraction patterns showed that SMSV crystals belong to I23 space group with cell dimensions a=b=c=457 A. The crystallographic asymmetric unit includes five icosahedral asymmetric units, each consisting of three capsid protein subunits. In the space group I23, given the icosahedral symmetry and the size of the virus particle, the location of the particle is constrained to be at the point where the crystallographic 2- and 3-fold axes intersect. The orientation of the virus particle in the unit cell was ascertained by self-rotation function calculations.
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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 [36]
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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
- Chen, R., Neill, J. D., & Venkataram Prasad, B. V.
- Affiliations
- Baylor College of Medicine (US)
- National Animal Disease Center (US)
- ORCID
- Neill, John D.
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 141
- Issue
- 2
- Pages
- 143-148
- ISSN
- 1047-8477 (ISSN-L)
- OpenAlex
- W2080099308
- Cited by
- 18
- References
- 0
- Citations by year
- 2020: 1 · 2019: 2 · 2018: 2 · 2016: 1 · 2015: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (R01AI38036)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- 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
- Keywords
- Caliciviridae, virus crystallization, X-ray crystallography, capsid protein, icosahedral symmetry, self-rotation function, single-stranded RNA viruses
- MeSH terms
- Capsid, Models, Molecular, X-Ray Diffraction, Vesicular exanthema of swine virus, Crystallography, X-Ray, Cell Culture Techniques, Cryoelectron Microscopy
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