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1 Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Dep. Biotecnología, Ctra Coruña Km 7.5, 28040 Madrid, Spain
2 Serveis Cientificotècnics (Unitat de Citometria de Flux), Parc Científic de Barcelona, Spain
3 CIQ(UP)/Departamento de Química, Faculdade de Ciências da Universidade do Porto, P-4169-007 Porto, Portugal
4 Protein Design Group, Centro Nacional de Biotecnología, Cantoblanco, 28049 Madrid, Spain
Correspondence
Victoria Ley
ley{at}inia.es
Heparan sulphate (HS) has been found to serve as receptor for initial cell binding of numerous viruses. Different glycosaminoglycans (GAGs), including heparin and HS, were analysed for their ability to bind swine vesicular disease virus (SVDV), a picornavirus with close homology to human coxsackie B5 virus. Binding of SVDV was established by heparin-affinity chromatography. In addition, infection of IB-RS-2 epithelial porcine cells was inhibited by treating the virus with soluble HS, heparin, and chondroitin sulphate B (CS-B), as well as by enzymic digestion of cell surface GAGs. Analysis of the infection course showed that SVDV uses cellular HS for its binding to the cell surface and that this interaction occurs during attachment of the virus, prior to its internalization into the cell. Sequence analysis of SVDV variants selected for their lack of sensitivity to heparin inhibition in vitro led to the identification of two residues (A2135V and I1266K) potentially involved in heparin/HS interaction. The location of these residues in a three-dimensional model shows that they are clustered in a well-exposed region of the capsid, providing a physical mechanism that could account for the heparin-binding phenotype.
Present address: Biomolecular Structure and Modelling Unit, Biochemistry and Molecular Biology Department, University College London, Gower Street, London WC1E 6BT, UK.
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