Abstract

In order to differentiate Epstein-Barr virus (EBV) strains by serological markers we prepared hybridomas producing monoclonal antibodies against polypeptides of the QIMR-WIL EBV strain. These monoclonal antibodies were screened by indirect immunofluorescence techniques. Immunoprecipitation using EBV-positive monoclonal antibodies and the protein A method, of 125I-labelled polypeptides from purified QIMR-WIL EBV particles, revealed that a series of monoclonal antibodies against the four main surface and envelope polypeptides precipitating p340, p340/p240, p140, and p80 were obtained. When 125I-labelled polypeptides from purified P3HR-1 and B95-8 EBV particles were immunoprecipitated, it could be demonstrated that several anti-p340 (QIMR-WIL) antibodies recognized strain-specific antigenic determinants, while anti-p340/p240 (QIMR-WIL) as well as anti-p140 (QIMR-WIL) antibody clones reacted with antigenic sites which are in common wither among B95-8 or in addition to P3HR-1 polypeptides. Thus, monoclonal antibodies now provide a serological basis for EBV typing.

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