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Mutational analysis of the Epstein—Barr virus nuclear antigen 2 by far-Western blotting and DNA-binding studies

¹ Institut für medizinische Mikrobiologie und Hygiene der Universitätskliniken des Saarlandes, Abteilung Virologie, Haus 47, 66421 Homburg/Saar, Germany,
² Department of Medicine, University of Washington and Veterans Administration Medical Center, Seattle, Washington, USA,
³ Division of Oncology, Department of Medicine, HSC T-17, 080, State University of New York Stony Brook, NY 11790-8174, USA,
⁴ Institut für Immunologie, Hämatologikum, GSF, Marchioninistrasse 25, 81377 München, Germany
and⁵ Institut für Klinische Molekularbiologie und Tumorgenetik, Hämatologikum, GSF, Marchioninistrasse 25, 81377 München, Germany

We have previously shown by far-Western blotting that the Epstein—Barr virus nuclear antigen 2 (EBNA-2) both binds to a cellular protein of 130 kDa and histone H1, with the complex between EBNA-2 and p130 being tighter than between EBNA-2 and histone H1. Here we demonstrate that the N terminus of EBNA-2, which was previously shown to be necessary for transformation of B lymphocytes by EBNA-2, is essential for binding to p130. We further show data indicating that the binding of EBNA-2 to histone H1 appears not to be mediated exclusively via the basic Arg-Gly rich region in the C-terminal part of EBNA-2. With a MAb directed against the Trp-Trp³²²-Pro (WWP) motif of EBNA-2, which is known to be essential for the interaction of EBNA-2 with the cellular factor RBPJ/CBF1, we could inhibit the DNA binding of EBNA-2, providing further evidence that this region of EBNA-2 forms direct contact with RBPJ/CBF1.

^* Author for correspondence. Fax +49 6841 16 3980. e-mail graesser@med-rz.uni-sb.de

Received 27 September 1995; accepted 19 December 1995.

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