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

• Type: Article in International Scientific Journal
• Date: 2004

Authors

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

Journal

Title: Journal of General Virology

Vol. 85

Pages: 653-663

ISSN: 0022-1317

Publisher: Microbiology Society

Indexing

ISI Web of Knowledge - 26 Citations

Scopus - 29 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11