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J Gen Virol 88 (2007), 177-186; DOI 10.1099/vir.0.82158-0

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© 2007 Society for General Microbiology

{alpha}2,6-Linked sialic acid acts as a receptor for Feline calicivirus

Amanda D. Stuart and T. David K. Brown

Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK

Correspondence
Amanda D. Stuart
ads35{at}mole.bio.cam.ac.uk

Feline calicivirus (FCV) is a major causative agent of respiratory disease in cats. It is also one of the few cultivatable members of the family Caliciviridae. It has recently been reported that FCV binding is in part due to interaction with junction adhesion molecule-A. This report describes the characterization of additional receptor components for FCV. Chemical treatment of cells with sodium periodate showed that FCV recognized carbohydrate moieties on the surface of permissive cells. Enzymic treatment with Vibrio cholerae neuraminidase demonstrated that sialic acid was a major determinant of virus binding. Further characterization using linkage-specific lectins from Maackia amurensis and Sambucus nigra revealed that FCV recognized sialic acid with an {alpha}2,6 linkage. Using various proteases and metabolic inhibitors, it was shown that {alpha}2,6-linked sialic acid recognized by FCV is present on an N-linked glycoprotein.




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