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J Gen Virol 55 (1981), 333-341; DOI 10.1099/0022-1317-55-2-333
© 1981 Society for General Microbiology
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Epstein—Barr Virus-induced Proteins. IV. Characterization of an EBV-associated Phosphopolypeptide

Nikolaus Mueller-Lantzsch{dagger} and Naoki Yamamoto

Institut für Virologie, Zentrum für Hygiene der Universität Freiburg, Hermann-Herder-Strasse 11, 78 Freiburg, West Germany

Cells of the Epstein—Barr virus (EBV) non-producing lines NC37 and Raji were induced by the tumour promoter TPA and were labelled with 32P. The analysis by immunoprecipitation with human VCA+EA+ sera revealed that a major phospho-polypeptide with a mol. wt. of 58000 was specifically precipitated. In addition, a phosphopolypeptide of the same size was the dominant phosphopolypeptide detected in EBV-producing B95-8 and P3HR-1 cells as well as in P3HR-1-superinfected NC37 cells. This phosphopolypeptide seemed to be EBV-specific, because it was not detectable in TPA-treated, but EBV genome-negative, Ramos and BJAB cells. Synthesis of this phosphopolypeptide was inhibited in TPA-treated NC37 cells by treatment with Ara-C. VCA+EA+ sera were found to be more immunoreactive with this phosphopolypeptide than VCA+EA- or EBNA+ sera. Based on these results this phosphopolypeptide may have some immunological relatedness to the EBV-specific early antigen (EA) complex defined by immunofluorescence.

Keywords: EBV proteins, TPA induction, immunoprecipitation

{dagger} Present address: Schweizerisches Serum und Impfinstitut, Bern, Switzerland.

Received 31 October 1980; accepted 2 March 1981.




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Copyright © 1981 by the Society for General Microbiology.