{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T23:23:29Z","timestamp":1787009009065,"version":"build-2736575974"},"reference-count":108,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2023,7,28]],"date-time":"2023-07-28T00:00:00Z","timestamp":1690502400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21K19373"],"award-info":[{"award-number":["21K19373"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21H02679"],"award-info":[{"award-number":["21H02679"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,10,6]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Sialic acid-binding immunoglobulin-like lectins (Siglecs) are a family of membrane molecules that recognize sialic acid. Most of them are inhibitory receptors that inhibit immune-cell activation by recognizing sialic acid as a self-motif. Human B cells express CD22 (also known as Siglec-2), Siglec-5, Siglec-6 and Siglec-10 whereas mouse B cells express CD22 and Siglec-G (ortholog of human Siglec-10). Siglecs recognize both sialylated molecules expressed on the same cell (cis-ligands) and those expressed by other cells (trans-ligands). In Guillain\u2013Barr\u00e9 syndrome (GBS), antibody production to gangliosides (which are sialic acid-containing glycolipids) expressed by neurons plays a pathogenic role. A Siglec-10 variant deficient in recognition of gangliosides is genetically associated with GBS, suggesting that Siglec-10 induces self-tolerance to gangliosides by recognizing gangliosides as trans-ligands. Recognition of the BCR as a cis-ligand by Siglec-G and CD22 suppresses BCR signaling in B-1 cells and conventional B cells, respectively. This signal suppression prevents excess expansion of B-1 cells and is involved in the quality control of signaling-competent B cells by setting a threshold for tonic signaling during B cell development. CD22 recognizes other cis-ligands including CD22 and \u03b27 integrin. Interaction of CD22 with other CD22 molecules induces CD22 clustering that suppresses CD22-mediated signal inhibition upon BCR ligation, and interaction with \u03b27 integrin maintains its function in the gut-homing of B cells. Taken together, interactions of B cell Siglecs with multiple trans- and cis-ligands play important roles in B cell homeostasis and immune responses.<\/jats:p>","DOI":"10.1093\/intimm\/dxad030","type":"journal-article","created":{"date-parts":[[2023,7,26]],"date-time":"2023-07-26T09:00:14Z","timestamp":1690362014000},"page":"461-473","source":"Crossref","is-referenced-by-count":10,"title":["The ligand interactions of B cell Siglecs are involved in the prevention of autoimmunity to sialylated self-antigens and in the quality control of signaling-competent B cells"],"prefix":"10.1093","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0760-1258","authenticated-orcid":false,"given":"Takeshi","family":"Tsubata","sequence":"first","affiliation":[{"name":"Department of Pathology, Nihon University School of Dentistry , 1-8-13 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-8310 , Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2023,7,28]]},"reference":[{"key":"2023100706570922100_CIT0001","doi-asserted-by":"crossref","first-page":"101117","DOI":"10.1016\/j.mam.2022.101117","article-title":"Discovery, classification, evolution and diversity of Siglecs","volume":"90","author":"Angata","year":"2022","journal-title":"Mol Aspects Med"},{"key":"2023100706570922100_CIT0002","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1021\/bi1014453","article-title":"Substrate specificity of protein tyrosine phosphatases 1B, RPTPalpha, SHP-1, and SHP-2","volume":"50","author":"Ren","year":"2011","journal-title":"Biochemistry"},{"key":"2023100706570922100_CIT0003","doi-asserted-by":"crossref","first-page":"2717","DOI":"10.4049\/jimmunol.162.5.2717","article-title":"Expression of dominant-negative src-homology domain 2-containing protein tyrosine phosphatase-1 results in increased Syk tyrosine kinase activity 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