Heparan sulphate mediates swine vesicular disease virus attachment to the host cell

• Tipo: Artigo em Revista Científica Internacional
• Data: 2004

Autores

Escribano Romero, E (Autor) Outra; Jimenez Clavero, MA (Autor) Outra; Gomes, P (Autor) FCUP; Garcia Ranea, JA (Autor) Outra; Ley, V (Autor) Outra

Revista

Título: Journal of General Virology

Vol. 85

Páginas: 653-663

ISSN: 0022-1317

Editora: Microbiology Society

Indexação

ISI Web of Knowledge - 26 Citações

Scopus - 29 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-000-BEM

DOI: 10.1099/vir.0.19603-0

Abstract (EN): 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 11 266K) 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 11