Structural insights into calicivirus attachment and uncoating.
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.
Medical Research Council Virology Unit, Glasgow University, Church St., Glasgow G11 5JR, United Kingdom. d.bhella@mrcvu.gla.ac.uk
David
D
Bhella
Derek
D
Gatherer
Yasmin
Y
Chaudhry
Rebecca
R
Pink
Ian G
IG
Goodfellow
D000818:Animals; D002139:Caliciviridae / Q000378:metabolism*; D017927:Calicivirus, Feline / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry*; D002415:Cats; D002448:Cell Adhesion; D020285:Cryoelectron Microscopy; D000939:Epitopes / Q000737:chemistry; D007091:Image Processing, Computer-Assisted; D007668:Kidney / Q000821:virology; D008854:Microscopy, Electron; D008968:Molecular Conformation; D011134:Polysaccharides / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D000939:Epitopes; D011134:Polysaccharides