Monoclonal antibodies against regions topologically surrounding the homodimeric β-barrel interface of Epstein-Barr virus nuclear antigen-1

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)87-94
Number of pages8
JournalVirus Research
Volume109
Issue number1
DOIs
StatePublished - Jan 1 2005

Keywords

  • EBNA-1
  • EBV
  • Homodimeric β-barrel
  • mAbs

ASJC Scopus subject areas

  • Cancer Research
  • Virology
  • Infectious Diseases

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