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

doi:10.1016/j.virusres.2004.10.012

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

Microbiology-Immunology

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	87-94
Number of pages	8
Journal	Virus Research
Volume	109
Issue number	1
DOIs	https://doi.org/10.1016/j.virusres.2004.10.012
State	Published - Apr 2005

Keywords

EBNA-1
EBV
Homodimeric β-barrel
mAbs

ASJC Scopus subject areas

Infectious Diseases
Cancer Research
Virology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.virusres.2004.10.012

Cite this

Eda, H., Ishii, Y., Obayashi, M., Harada, S., Ito, S., Fujita, T., Ikeda, M., Kusano, S., Kitamura, R., Suzuki, C., Hara, T., Watanabe, M., Satoh, H., Sugihara, K., & Yanagi, K. (2005). Monoclonal antibodies against regions topologically surrounding the homodimeric β-barrel interface of Epstein-Barr virus nuclear antigen-1. Virus Research, 109(1), 87-94. https://doi.org/10.1016/j.virusres.2004.10.012

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

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.",

keywords = "EBNA-1, EBV, Homodimeric β-barrel, mAbs",

author = "Hiroyuki Eda and Yasuyuki Ishii and Maya Obayashi and Shizuko Harada and Sayuri Ito and Tomomichi Fujita and Masato Ikeda and Shuichi Kusano and Ryo Kitamura and Chieko Suzuki and Takahiko Hara and Motoo Watanabe and Hiroshi Satoh and Keisuke Sugihara and Kazuo Yanagi",

year = "2005",

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doi = "10.1016/j.virusres.2004.10.012",

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volume = "109",

pages = "87--94",

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Eda, H, Ishii, Y, Obayashi, M, Harada, S, Ito, S, Fujita, T, Ikeda, M, Kusano, S, Kitamura, R, Suzuki, C, Hara, T, Watanabe, M, Satoh, H, Sugihara, K & Yanagi, K 2005, 'Monoclonal antibodies against regions topologically surrounding the homodimeric β-barrel interface of Epstein-Barr virus nuclear antigen-1', Virus Research, vol. 109, no. 1, pp. 87-94. https://doi.org/10.1016/j.virusres.2004.10.012

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AU - Eda, Hiroyuki

AU - Ishii, Yasuyuki

AU - Obayashi, Maya

AU - Harada, Shizuko

AU - Ito, Sayuri

AU - Fujita, Tomomichi

AU - Ikeda, Masato

AU - Kusano, Shuichi

AU - Kitamura, Ryo

AU - Suzuki, Chieko

AU - Hara, Takahiko

AU - Watanabe, Motoo

AU - Satoh, Hiroshi

AU - Sugihara, Keisuke

AU - Yanagi, Kazuo

PY - 2005/4

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N2 - 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.

AB - 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.

KW - EBNA-1

KW - EBV

KW - Homodimeric β-barrel

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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