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Structural insights into calicivirus attachment and uncoating

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • David Bhella
  • Derek Gatherer
  • Yasmin Chaudhry
  • Rebecca Pink
  • Ian G. Goodfellow
<mark>Journal publication date</mark>08/2008
<mark>Journal</mark>Journal of Virology
Issue number16
Number of pages8
Pages (from-to)8051-8058
Publication StatusPublished
<mark>Original language</mark>English


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.