Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9289493 | Virus Research | 2005 | 8 Pages |
Abstract
Epstein-Barr virus (EBV) nuclear antigen-1 (EBNA-1) is essential for maintenance of EBV latency. Four mouse monoclonal antibodies (mAbs) against the part of the EBNA-1 sequence (amino acids 451-641) containing the domain that forms a homodimeric eight-stranded β-barrel were generated and characterized, examined for immunocytochemical staining, immunoblotting and isoelectric focusing of EBNA-1 proteins, and used to examine interactions between EBNA-1 polypeptides by far-Western blot assays. Far-Western blot analyses using the mAbs suggest that both the β-strand (aa 593-604) and α helix (aa 568-582) are essential for EBNA-1 dimerization, consistent with yeast two-hybrid studies of mutant EBNA-1 polypeptides. These mAbs should be useful for studies on the structure and function of EBNA-1 proteins.
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Authors
Hiroyuki Eda, Yasuyuki Ishii, Maya Obayashi, Shizuko Harada, Sayuri Ito, Tomomichi Fujita, Masato Ikeda, Shuichi Kusano, Ryo Kitamura, Chieko Suzuki, Takahiko Hara, Motoo Watanabe, Hiroshi Satoh, Keisuke Sugihara, Kazuo Yanagi,