Use of fluoresceinated Epstein-Barr virus to study Epstein-Barr virus-lymphoid cell interactions

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Abstract
As a direct approach to visualize Epstein-Barr virus (EBV) binding to its cellular receptors and to learn more on the nature of this binding, virus preparations were conjugated to fluorescein isothiocyanate and used to detect EBV receptors on lymphoid cells. Different enzymatic and chemical treatments were also applied either to the virus or to target cells or to both, and the effect of these treatments on virus binding was examined. EBV can be fluoresceinated without affecting its infectivity or cell binding ability and the fluoresceinated virus represents an important tool to investigate the biology and nature of EBV interactions with its cellular receptors; the 2 virus strains (P3HR-1 and B95-8) share common receptors on Raji [human lymphoblastoid] cells; protease treatment of EBV or target cells abrogates virus binding; EBV receptors regenerate after removal of the protease and this regeneration is inhibited by cycloheximide or sucrose; EBV particles bear concanavalin A receptors and this lectin hinders the interaction of the virus with its cellular receptors; neuraminidase treatment, various monosaccharides, ovalbumin and glycopeptides derived from EBV or cell surface do not inhibit virus binding. Thus, some cellular and viral surface (glyco-) proteins are required for EBV binding to its targets.

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