Functional cross-reactivity between the glycoprotein B of herpes simplex virus type 1 and Epstein-Barr virus.

A monoclonal antibody (T157) directed against gB-1, the glycoprotein B (gB) of herpes simplex virus-1 (HSV-1) shows positive indirect immunoflourescent staining with an Epstein-Barr virus (EBV)-transformed lymphoblastoid cell line B95-8. SDS PAGE and Western blot analysis show that B95-8 cells contain a 110,000 MW protein that co-migrates with the 110,000-115,000 MW gB-1. The gB-1 homologue of EBV (gB-EBV), immunopurified using a T157 affinity column, cross-stimulates HSV-1 immune T cells to proliferate in vitro. Mice immunized by a single subcutaneous injection of 30 microg gB-EBV in saline developed significant protection against HSV-1 challenge infection. Therefore gB-EBV can be considered a potential candidate vaccine and as an antigen to examine the cell-mediated immune response mounted by the host to limit virus spread during productive infection. The significance of a better understanding of the immune response to this and other EBV proteins of productive infection as an alternative to limit tumour growth by preventing virus spread is discussed.