Structural insights into calicivirus attachment and uncoating

Bhella, D. , Gatherer, D., Chaudhry, Y., Pink, R. and Goodfellow, I.G. (2008) Structural insights into calicivirus attachment and uncoating. Journal of Virology, 82(16), pp. 8051-8058. (doi:10.1128/JVI.00550-08)

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Publisher's URL: http://dx.doi.org/10.1128/JVI.00550-08

Abstract

The Caliciviridae family comprises positive-sense RNA viruses of medical and veterinary significance. In humans, caliciviruses are a major cause of acute gastroenteritis, while in animals respiratory illness, conjunctivitis, stomatitis, and hemorrhagic disease are documented. Investigation of virus-host interactions is limited by a lack of culture systems for many viruses in this family. Feline calicivirus (FCV), a member of the Vesivirus genus, provides a tractable model, since it may be propagated in cell culture. Feline junctional adhesion molecule 1 (fJAM-1) was recently identified as a functional receptor for FCV. We have analyzed the structure of this virus-receptor complex by cryo-electron microscopy and three-dimensional image reconstruction, combined with fitting of homology modeled high-resolution coordinates. We show that domain 1 of fJAM-1 binds to the outer face of the P2 domain of the FCV capsid protein VP1, inducing conformational changes in the viral capsid. This study provides the first structural view of a native calicivirus-protein receptor complex and insights into the mechanisms of virus attachment and uncoating

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Gatherer, Dr Derek and Bhella, Dr David
Authors: Bhella, D., Gatherer, D., Chaudhry, Y., Pink, R., and Goodfellow, I.G.
Subjects:Q Science > QR Microbiology > QR355 Virology
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Research Group:MRC Virology
Journal Name:Journal of Virology
Journal Abbr.:J. Virol.
ISSN:0022-538X
ISSN (Online):1098-5514

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