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Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILR alpha immune cell receptor

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タイトル: Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILR alpha immune cell receptor
著者: Furukawa, Atsushi 著作を一覧する
Kakita, Kosuke 著作を一覧する
Yamada, Tomoki 著作を一覧する
Ishizuka, Mikihiro 著作を一覧する
Sakamoto, Jiro 著作を一覧する
Hatori, Nanao 著作を一覧する
Maeda, Naoyoshi 著作を一覧する
Ohsaka, Fumina 著作を一覧する
Saitoh, Takashi 著作を一覧する
Nomura, Takao 著作を一覧する
Kuroki, Kimiko 著作を一覧する
Nambu, Hisanori 著作を一覧する
Arase, Hisashi 著作を一覧する
Matsunaga, Shigeki 著作を一覧する
Anada, Masahiro 著作を一覧する
Ose, Toyoyuki 著作を一覧する
Hashimoto, Shunichi 著作を一覧する
Maenaka, Katsumi 著作を一覧する
発行日: 2017年12月22日
出版者: American Society for Biochemistry and Molecular Biology (ASBMB)
誌名: Journal of Biological Chemistry (JBC)
巻: 292
号: 51
開始ページ: 21128
終了ページ: 21136
出版社 DOI: 10.1074/jbc.M117.799239
抄録: Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor alpha (PILR alpha) on immune cells. PILR alpha belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)- like family, members of which bind SA. PILR alpha is the only Siglec member to recognize not only the sialylated O-linked sugar T antigen (sTn) but also its attached peptide region. We previously determined the crystal structure of PILR alpha complexed with the sTn-linked glycopeptide of glycoprotein B, revealing the simultaneous recognition of sTn and peptide by the receptor. However, the contribution of each glycopeptide component to PILR alpha binding was largely unclear. Here, we chemically synthesized glycopeptide derivatives and determined the thermodynamic parameters of their interaction with PILR alpha. We show that glycopeptides with different sugar units linking SA and peptides (i.e. "GlcNAc-type" and "deoxy-GlcNAc-type" glycopeptides) have lower affinity and more enthalpy-driven binding than the wild type (i.e. GalNAc-type glycopeptide). The crystal structures of PILR alpha complexed with these glycopeptides highlighted the importance of stereochemical positioning of the O4 atom of the sugar moiety. These results provide insights both for understanding the unique O-glycosylated peptide recognition by the PILR alpha and for the rational design of herpes simplex virus-1 entry inhibitors.
Rights: This research was originally published in JBC. Furukawa, Atsushi et al. Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILR alpha immune cell receptor. Journal of Biological Chemistry. 2017; 292:21128-21136. © the American Society for Biochemistry and Molecular Biology.
資料タイプ: article
URI: http://hdl.handle.net/2115/72215
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 前仲 勝実

 

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