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Related Experiment Video

Updated: Jul 4, 2026

Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

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Published on: July 15, 2019

Structural insights into calicivirus attachment and uncoating.

David Bhella¹, Derek Gatherer, Yasmin Chaudhry

¹Medical Research Council Virology Unit, Glasgow University, Church St., Glasgow G11 5JR, United Kingdom. d.bhella@mrcvu.gla.ac.uk

Journal of Virology

|June 14, 2008

Summary

Researchers visualized the feline calicivirus (FCV) structure bound to its receptor, feline junctional adhesion molecule 1 (fJAM-1). This reveals how the virus attaches and changes shape, offering insights into calicivirus infections.

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Area of Science:

Virology
Structural Biology
Molecular Interactions

Background:

Caliciviridae are significant RNA viruses causing human gastroenteritis and animal diseases.
Studying virus-host interactions is challenging due to limited culture systems for many caliciviruses.
Feline calicivirus (FCV) is a model virus, cultivable in vitro, with feline junctional adhesion molecule 1 (fJAM-1) identified as its receptor.

Purpose of the Study:

To determine the structural basis of the interaction between FCV and its host cell receptor, fJAM-1.
To elucidate the mechanism of FCV attachment to host cells at a molecular level.

Main Methods:

Cryo-electron microscopy and 3D image reconstruction were employed.
Homology modeling was used to fit high-resolution coordinates into the reconstructed map.
Structural analysis of the virus-receptor complex was performed.

Main Results:

The structure of the native calicivirus-protein receptor complex was determined for the first time.
Domain 1 of fJAM-1 was shown to bind the P2 domain of the FCV capsid protein VP1.
This binding induces conformational changes in the viral capsid.

Conclusions:

This study provides the first structural insights into calicivirus-receptor interactions.
The findings illuminate the mechanisms of FCV attachment and subsequent uncoating.
Understanding these interactions is crucial for developing antiviral strategies against caliciviruses.