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Structural insights into calicivirus attachment and uncoating

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Structural insights into calicivirus attachment and uncoating. / Bhella, David; Gatherer, Derek; Chaudhry, Yasmin et al.
In: Journal of Virology, Vol. 82, No. 16, 08.2008, p. 8051-8058.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Bhella, D, Gatherer, D, Chaudhry, Y, Pink, R & Goodfellow, IG 2008, 'Structural insights into calicivirus attachment and uncoating', Journal of Virology, vol. 82, no. 16, pp. 8051-8058. https://doi.org/10.1128/JVI.00550-08

APA

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

Vancouver

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

Author

Bhella, David ; Gatherer, Derek ; Chaudhry, Yasmin et al. / Structural insights into calicivirus attachment and uncoating. In: Journal of Virology. 2008 ; Vol. 82, No. 16. pp. 8051-8058.

Bibtex

@article{58fcc94bbd1d4f5892243666f4c89156,
title = "Structural insights into calicivirus attachment and uncoating",
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.",
keywords = "Animals, Caliciviridae, Calicivirus, Feline, Capsid, Cats, Cell Adhesion, Cryoelectron Microscopy, Epitopes, Image Processing, Computer-Assisted, Kidney, Microscopy, Electron, Molecular Conformation, Polysaccharides, Protein Binding, Protein Structure, Tertiary",
author = "David Bhella and Derek Gatherer and Yasmin Chaudhry and Rebecca Pink and Goodfellow, {Ian G.}",
year = "2008",
month = aug,
doi = "10.1128/JVI.00550-08",
language = "English",
volume = "82",
pages = "8051--8058",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "16",

}

RIS

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 -