Purification of herpes simplex virus glycoproteins B and C using monoclonal antibodies and their ability to protect mice against lethal challenge.

Monoclonal antibodies which react with herpes simplex virus type 1 (HSV-1) glycoproteins, but do not neutralize infectivity, were prepared. The protein to which each monoclonal antibody was directed was determined by various techniques including their reaction with polypeptides from glycoprotein-deficient mutants after protein blotting, and also tests using passive haemagglutination. Monoclonal antibodies A7 and alpha C3 were directed against a type-specific determinant on gC and a type-common determinant on gB respectively. In addition, A7 reacted only with the HFEM strain of HSV-1 and did not react with any of the 20 low-passage human isolates also tested. The monoclonal antibodies were used in immunoadsorption chromatography to purify individual glycoproteins from detergent extracts of HSV-1-infected cells. The ability of the monoclonal antibodies or purified glycoproteins to protect mice against a lethal encephalitis induced by intracerebral inoculation of HSV-1 was investigated. Passive immunization was not very effective; however, purified gC or a mixture of gB and its precursor pgB induced good levels of neutralizing antibody which persisted for at least 9 weeks and mice survived virus challenge.