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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.
- Source :
-
International Immunology . Oct2023, Vol. 35 Issue 10, p461-473. 13p. - Publication Year :
- 2023
-
Abstract
- 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–Barré 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 β7 integrin. Interaction of CD22 with other CD22 molecules induces CD22 clustering that suppresses CD22-mediated signal inhibition upon BCR ligation, and interaction with β7 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09538178
- Volume :
- 35
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- International Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 172851977
- Full Text :
- https://doi.org/10.1093/intimm/dxad030