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Preparative SDS-PAGE Electrophoresis of a Recombinant Epstein-Barr Virus Encoded Protein and Its Application in Serodiagnostic Test Systems, Rev C

able to improve sensitivity as well as specificity of derivative test systems. In general, the production of recombinant antigens for diagnostic purposes is inexpensive compared to the use of purified natural antigens. The major problems associated with such test systems are identification of viral antigens that guarantee a certain serological diagnosis, their expression, and, most importantly, the subsequent purification of the recombinant proteins to near homogeneity. Epstein-Barr virus (EBV) is an ubiquitous human B-lymphotropic herpesvirus. It is the causative agent of infectious mononucleosis, a mostly self-limiting lymphoproliferative disease, and is closely associated with an increasing number of severe human malignancies. Therefore, an early and accurate diagnosis as well as the follow-up of severe infections are of vital importance.

Previous experiments by our group led to identification of a 23 kD viral protein recognized by antibodies from more than 96% of EBV carriers tested. After identification of the coding region, the corresponding fragment of the viral genome was cloned into a suitable prokaryotic expression vector and, following a careful optimization process, the recombinant protein was expressed in E. coli cells at a very high level.

Here we report the large-scale purification of the EBV-encoded 23 kD protein to near homogeneity by a combination of ureasolubilization and preparative continuous elution SDS-PAGE electrophoresis using the Bio-Rad Model 491 prep cell device. Following prep cell purification, the recombinant antigen was ready to use in serodiagnostic test systems. The presented purification strategy can be adapted to a variety of recombinant proteins.


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