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- W3197431482 abstract "Siglec-1, also known as Sialoadhesin (Sn) and CD169 is highly conserved among vertebrates and with 17 immunoglobulin-like domains is Siglec-1 the largest member of the Siglec family. Expression of Siglec-1 is found primarily on dendritic cells (DCs), macrophages and interferon induced monocyte. The structure of Siglec-1 is unique among siglecs and its function as a receptor is also different compared to other receptors in this class as it contains the most extracellular domains out of all the siglecs. However, the ability of Siglec-1 to internalize antigens and to pass them on to lymphocytes by allowing dendritic cells and macrophages to act as antigen presenting cells, is the main reason that has granted Siglec-1's key role in multiple human disease states including atherosclerosis, coronary artery disease, autoimmune diseases, cell-cell signaling, immunology, and more importantly bacterial and viral infections. Enveloped viruses for example have been shown to manipulate Siglec-1 to increase their virulence by binding to sialic acids present on the virus glycoproteins allowing them to spread or evade immune response. Siglec-1 mediates dissemination of HIV-1 in activated tissues enhancing viral spread via infection of DC/T-cell synapses. Overall, the ability of Siglec-1 to bind a variety of target cells within the immune system such as erythrocytes, B-cells, CD8+ granulocytes and NK cells, highlights that Siglec-1 is a unique player in these essential processes." @default.
- W3197431482 created "2021-09-13" @default.
- W3197431482 creator A5027795204 @default.
- W3197431482 creator A5028708552 @default.
- W3197431482 creator A5030695851 @default.
- W3197431482 creator A5068849696 @default.
- W3197431482 creator A5070167637 @default.
- W3197431482 creator A5074413996 @default.
- W3197431482 date "2021-09-08" @default.
- W3197431482 modified "2023-10-16" @default.
- W3197431482 title "The role of sialic acid-binding immunoglobulin-like-lectin-1 (siglec-1) in immunology and infectious disease" @default.
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