Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Virus or component thereof
Patent
1998-08-13
2000-12-19
Salimi, Ali R.
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Virus or component thereof
4242041, 4241861, 4241991, 4352351, 435325, 4353201, 435 5, 435 793, 514 13, 530233, 536 2372, A61K 39245, A61K 3912
Patent
active
061624403
ABSTRACT:
The present invention provides peptides having substantial homology with the CBF1/RBPJk interaction domain of EBNA2. The peptides preferably comprise between about ten and twenty amino acids. The peptides are able to compete with the native EBV EBNA2 protein for interaction with CBF1. The peptides thus can be employed as a pharmaceutical, e.g., along with an appropriate carrier in a pharmaceutical composition, particularly in a method of protecting against or treating EBV infection. The peptides also can be employed in a method of detecting factors that interact with the EBV EBNA2 protein.
REFERENCES:
Grossman et al., "The Epstein-Barr Virus Nuclear Antigen 2 Transactivator is Directed to Response Elements by the JK Recombination Signal Binding Protein," Proc. Natl. Acad. Sci., vol. 91, No. 16, pp. 7568-7572 (1994).
Henkel et al., "Mediation of Epstein-Barr Virus EBNA2 Transactivation by Recombination Signal-Binding Protein JK," Science, vol. 265, pp. 92-95 (1994).
Ling et al., "The Epstein-Barr Virus Immortalizating Protein EBNA-2 is Targeted to DNA by a Cellular Enhancer-Binding Protein," Proc. Natl. Acad. Sci., vol. 90, No. 20, pp. 9237-9241 (1993).
Ling et al., "Contribution of Conserved Amino Acids in Mediating the Interaction Between EBNA2 and CBFa/RBPJK," Journal of Virology, vol. 69, No. 3, pp. 1944-1950 (1995).
Yalamanchili et al., "Genetic and Biochemical Evidence that EBNA2 Interaction with a 63-kDa Cellular GTG-Binding Protein is Essential for B-lymphocyte Growth Transformation by EBV," Virology, vol. 204, No. 2, pp. 634-641 (1994).
Hayward S. Diane
Ling Paul Dalling
Johns Hopkins University School of Medicine
Salimi Ali R.
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