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oai:kanazawa-u.repo.nii.ac.jp:00060836 2024-06-20T06:49:11Z 1132:1133:1135

Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor 古川, 敦 30727699 Furukawa, Atsushi Kakita, Kosuke Yamada, Tomoki Ishizuka, Mikihiro Sakamoto, Jiro Hatori, Nanao Maeda, Naoyoshi Ohsaka, Fumina Saitoh, Takashi 80115261 Nomura, Takahiro Kuroki, Kimiko Nambu, Hisanori Arase, Hisashi Matsunaga, Shigeki Anada, Masahiro Ose, Toyoyuki Hashimoto, Shunichi Maenaka, Katsumi Copyright © 2017 Yamazaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. This is an Open Access article under the CC BY license. Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor α (PILRα) on immune cells. PILRα belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)- like family, members of which bind SA. PILRα 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 PILRα 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 PILRα binding was largely unclear. Here, we chemically synthesized glycopeptide derivatives and determined the thermodynamic parameters of their interaction with PILRα. 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 PILRα 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 PILRα and for the rational design of herpes simplex virus-1 entry inhibitors. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc. 金沢大学医薬保健研究域薬学系 American Society for Biochemistry and Molecular Biology Inc. 2017-12-22 2022-09-12 eng journal article VoR https://doi.org/10.24517/00067081 http://hdl.handle.net/2297/00067081 https://kanazawa-u.repo.nii.ac.jp/records/60836 10.24517/00067081 10.1074/jbc.M117.799239 https://www.sciencedirect.com/science/article/pii/S0021925820327617?via%3Dihub https://www.sciencedirect.com/science/article/pii/S0021925820327617?via%3Dihub https://www.journals.elsevier.com/journal-of-biological-chemistry https://www.journals.elsevier.com/journal-of-biological-chemistry http://www.asbmb.org/ http://www.asbmb.org/ AA00251083 0021-9258 1083-351X Journal of Biological Chemistry 292 51 21128 21136 https://kanazawa-u.repo.nii.ac.jp/record/60836/files/PH-PR-FURUKAWA-A-51-21128.pdf application/pdf 1.9 MB 2022-09-12