Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Structural insights into calicivirus attachment and uncoating
AU - Bhella, David
AU - Gatherer, Derek
AU - Chaudhry, Yasmin
AU - Pink, Rebecca
AU - Goodfellow, Ian G.
PY - 2008/8
Y1 - 2008/8
N2 - 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.
AB - 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.
KW - Animals
KW - Caliciviridae
KW - Calicivirus, Feline
KW - Capsid
KW - Cats
KW - Cell Adhesion
KW - Cryoelectron Microscopy
KW - Epitopes
KW - Image Processing, Computer-Assisted
KW - Kidney
KW - Microscopy, Electron
KW - Molecular Conformation
KW - Polysaccharides
KW - Protein Binding
KW - Protein Structure, Tertiary
U2 - 10.1128/JVI.00550-08
DO - 10.1128/JVI.00550-08
M3 - Journal article
C2 - 18550656
VL - 82
SP - 8051
EP - 8058
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 16
ER -