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Sialic acid acts as a receptor for equine rhinitis A virus binding and infection

Rachel A. Stevenson

Jin-an Huang

Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Parkville, VIC 3010, Australia

Correspondence
Carol A. Hartley
carolah{at}unimelb.edu.au

Equine rhinitis A virus (ERAV) is a member of the genus Aphthovirus, family Picornaviridae, and causes respiratory disease in horses worldwide. To characterize the putative receptor molecule(s) of the ERAV isolate 393/76 (ERAV.393/76) on the surface of Vero and other cells, an assay was developed to measure the binding of purified biotinylated ERAV.393/76 virions to cells by flow cytometry. Using this assay, the level of binding to different cell types correlated with the relative infectivity of ERAV in each cell type. In particular, equine fetal kidney cells, mouse fibroblast cells, rabbit kidney-13 and Crandell feline kidney cells bound virus at high levels and produced high virus yields (10⁷ TCID₅₀ ml^–1). Madin–Darby bovine kidney and baby hamster kidney cells showed little or no binding of virus, producing yields of 10^1·8 TCID₅₀ ml^–1. Treatment of Vero and other cells with sodium periodate and the metabolic inhibitors tunicamycin, benzyl N-acetyl--D-galactosamide, D,L-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol and proteases indicated that part of the receptor-binding and entry complex for ERAV.393/76 is on N-linked carbohydrates and that the carbohydrate is likely to be present on a protein rather than a lipid backbone. The effect of carbohydrate-specific lectins and neuraminidases on ERAV.393/76 binding and infection of Vero and other cell types implicated 2,3-linked sialic acid residues on the carbohydrate complex in the binding and infection of ERAV.

Present address: Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia.

Present address: Pfizer, Animal Health R & D, 45 Poplar Road, Parkville, VIC 3052, Australia.

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