{"created":"2023-07-27T07:00:46.947922+00:00","id":60835,"links":{},"metadata":{"_buckets":{"deposit":"cbf8802a-3fcb-4c1a-a066-86d462a74cac"},"_deposit":{"created_by":18,"id":"60835","owners":[18],"pid":{"revision_id":0,"type":"depid","value":"60835"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00060835","sets":["1132:1133:1135"]},"author_link":["106980","106971","106953","106954","106943","106955","87685","87686","106979"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2020-07-10","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"28","bibliographicPageEnd":"9541","bibliographicPageStart":"9531","bibliographicVolumeNumber":"295","bibliographic_titles":[{"bibliographic_title":"Journal of Biological Chemistry"}]}]},"item_4_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"古川, 敦"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"平安, 恒幸"}],"nameIdentifiers":[{},{}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Human leukocyte immunoglobulin-like receptors (LILRs) typically regulate immune activation by binding to the human leukocyte antigen class I molecules. LILRA2, a member of the LILR family, was recently reported to bind to other unique ligands, the bacterially degraded Igs (N-truncated Igs), for the activation of immune cells. Therefore, LILRA2 is currently attracting significant attention as a novel innate immune receptor. However, the detailed recognition mechanisms required for this interaction remain unclear. In this study, using several biophysical techniques, we uncovered the molecular mechanism of N-truncated Ig recognition by LILRA2. Surface plasmon resonance analysis disclosed that LILRA2 specifically binds to N-truncated Ig with weak affinity (Kd = 4.8 mM) and fast kinetics. However, immobilized LILRA2 exhibited a significantly enhanced interaction with N-truncated Ig due to avidity effects. This suggests that cell surface-bound LILRA2 rapidly monitors and identifies bi- or multivalent abnormal N-truncated Igs through specific cross-linking to induce immune activation. Van't Hoff analysis revealed that this interaction is enthalpy-driven, with a small entropy loss, and results from differential scanning calorimetry indicated the instability of the putative LILRA2-binding site, the Fab region of the N-truncated Ig. Atomic force microscopy revealed that N truncation does not cause significant structural changes in Ig. Furthermore, mutagenesis analysis identified the hydrophobic region of LILRA2 domain 2 as the N-truncated Ig-binding site, representing a novel ligand-binding site for the LILR family. These results provide detailed insights into the molecular regulation of LILR-mediated immune responses targeting ligands that have been modified by bacteria. © 2020 Yamazaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.","subitem_description_type":"Abstract"}]},"item_4_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"金沢大学医薬保健研究域薬学系","subitem_description_type":"Other"}]},"item_4_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00067080","subitem_identifier_reg_type":"JaLC"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"American Society for Biochemistry and Molecular Biology Inc."}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1074/jbc.ra120.013354","subitem_relation_type_select":"DOI"}}]},"item_4_relation_28":{"attribute_name":"関連URI","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"https://www.sciencedirect.com/science/article/pii/S002192581748971X?via%3Dihub"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.sciencedirect.com/science/article/pii/S002192581748971X?via%3Dihub","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"https://www.journals.elsevier.com/journal-of-biological-chemistry"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.journals.elsevier.com/journal-of-biological-chemistry","subitem_relation_type_select":"URI"}},{"subitem_relation_name":[{"subitem_relation_name_text":"http://www.asbmb.org/"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"http://www.asbmb.org/","subitem_relation_type_select":"URI"}}]},"item_4_rights_23":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Copyright ©  2020 Yamazaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc."},{"subitem_rights":"This is an Open Access article under the CC BY license."}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA00251083","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0021-9258","subitem_source_identifier_type":"ISSN"},{"subitem_source_identifier":"1083-351X","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Yamazaki, Rika"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Furukawa, Atsushi"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Hirayasu, Kouyuki"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Yumoto, Kohei"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Fukuhara, Hideo"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Arase, Hisashi"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Maenaka, Katsumi"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2022-09-12"}],"displaytype":"detail","filename":"PH-PR-FURUKAWA-A-295-9531.pdf","filesize":[{"value":"1.5 MB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"PH-PR-FURUKAWA-A-295-9531.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/60835/files/PH-PR-FURUKAWA-A-295-9531.pdf"},"version_id":"13455fb6-6e97-44a4-9d2a-fd9baf59d629"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2"}]},"item_type_id":"4","owner":"18","path":["1135"],"pubdate":{"attribute_name":"公開日","attribute_value":"2022-09-12"},"publish_date":"2022-09-12","publish_status":"0","recid":"60835","relation_version_is_last":true,"title":["Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2"],"weko_creator_id":"18","weko_shared_id":-1},"updated":"2023-07-27T10:13:30.658096+00:00"}