1887

Abstract

(FCV) is a major causative agent of respiratory disease in cats. It is also one of the few cultivatable members of the family . 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 neuraminidase demonstrated that sialic acid was a major determinant of virus binding. Further characterization using linkage-specific lectins from and revealed that FCV recognized sialic acid with an 2,6 linkage. Using various proteases and metabolic inhibitors, it was shown that 2,6-linked sialic acid recognized by FCV is present on an -linked glycoprotein.

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2007-01-01
2019-12-13
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