Role of the extracellular domain of human herpesvirus 7 glycoprotein B in virus binding to cell surface heparan sulfate proteoglycans.

摘要: In an attempt to identify the human herpesvirus 7 (HHV-7) envelope protein(s) involved in cell surface binding, extracellular domain of HHV-7 glycoprotein B (gB) homolog protein was cloned and expressed as a fusion product with Fc immunoglobulin G heavy chain gamma1 (gB-Fc) eukaryotic system. Indirect immunofluorescence followed by flow cytometric analysis revealed specific binding gB-Fc membrane SupT1 cells but not other CD4+ T-lymphoblastoid lines, such Jurkat or PM1, clearly indicating that did bind CD4 molecule. This also suggested ability CD4-negative fibroblastoid Chinese hamster ovary (CHO) cells. The abrogated enzymatic removal heparan sulfate proteoglycans heparinase heparitinase treatment condroitinase ABC. addition, CHO severely impaired presence soluble heparin, well when sulfate-deficient mutant were used. Consistent these findings, heparin found block infection syncytium formation line. Although antigen is critical component receptor for T-lymphotropic HHV-7, findings suggest heparin-like molecules play important role HHV-7-cell interactions required gB represents one proteins adsorption virus-to-cell proteoglycans.