This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Epstein, A L Search for Related Content PubMed PubMed Citation Articles by Epstein, A L

 Previous Article  |  Next Article 

J Virol. 1984 May; 50(2): 372-379

Immunobiochemical characterization with monoclonal antibodies of Epstein-Barr virus-associated early antigens in chemically induced cells.

ABSTRACT

Five monoclonal antibodies which are reactive to early antigens of Epstein-Barr virus have been produced by using somatic cell hybridization techniques. The specificity of the monoclonal antibodies to early antigens was demonstrated by indirect immunofluorescence, which showed that the antigens were localized to the nucleus of early antigen-induced Raji cells. Additional indirect immunofluorescence studies showed that like patient antisera to diffuse-staining early antigen, the monoclonal antibodies gave positive staining reactions after methanol fixation. One of the antibodies, 1150-4, was positive by the anti-complement immunofluorescence technique but differed with Epstein-Barr virus-associated nuclear antigen-positive patient sera in that it only stained induced cells. Different fixation methods were found to alter dramatically the appearance of the nuclear staining reactions produced by the monoclonal antibodies. Immunoprecipitation and immunoblot experiments revealed that monoclonal antibodies 1108-1 and 1129-1 recognized two polypeptides of 55,000 and 50,000 daltons (p55;50), 1173-6 and 1180-2 recognized just p50, and 1150-4 identified a 65,000-dalton nuclear protein. Immunobiochemical characterization of these viral antigens showed that p55 is a phosphoprotein, and p55;50 has strong DNA-binding activity preferentially to single-stranded DNA. Elucidation of the role of these nuclear proteins in Epstein-Barr virus infection and the events associated with Epstein-Barr virus-directed lymphocyte transformation may provide significant information on the pathogenicity of this important human virus.

This article has been cited by other articles:

• Davido, D. J., von Zagorski, W. F., Maul, G. G., Schaffer, P. A. (2003). The Differential Requirement for Cyclin-Dependent Kinase Activities Distinguishes Two Functions of Herpes Simplex Virus Type 1 ICP0. J. Virol. 77: 12603-12616 [Abstract] [Full Text]  
• Gershburg, E., Pagano, J. S. (2002). Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the L-Riboside Benzimidazole 1263W94. J. Virol. 76: 998-1003 [Abstract] [Full Text]  
• Cao, T, Duprez, E, Borden, K., Freemont, P., Etkin, L. (1998). Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. J. Cell Sci. 111: 1319-1329 [Abstract]  
• Day, P. M., Roden, R. B. S., Lowy, D. R., Schiller, J. T. (1998). The Papillomavirus Minor Capsid Protein, L2, Induces Localization of the Major Capsid Protein, L1, and the Viral Transcription/Replication Protein, E2, to PML Oncogenic Domains. J. Virol. 72: 142-150 [Abstract] [Full Text]  
• Sternsdorf, T., Jensen, K., Zuchner, D., Will, H. (1997). Cellular Localization, Expression, and Structure of the Nuclear Dot Protein 52. J. Cell Biol. 138: 435-448 [Abstract] [Full Text]