Signaling lymphocytic activation molecule family member 1 (SLAMF1) (CD150)

Signaling lymphocytic activation molecule family member 1 (SLAMF1), also known as CD150, is a cell surface glycoprotein expressed on various hematopoietic cells, including T cells, B cells, dendritic cells, and macrophages [1, 2]. It functions as a homophilic receptor, meaning it acts as its own ligand to mediate cell-cell interactions and provide costimulatory signals that enhance lymphocyte activation and cytokine production, particularly interferon-gamma [1, 3, 5]. Beyond its role in normal immunity, CD150 is the primary entry receptor for wild-type measles virus, which binds to the extracellular domain to infect host cells [6, 14]. In clinical oncology, CD150 expression serves as a significant prognostic biomarker in chronic lymphocytic leukemia (CLL), where higher levels are often associated with a more favorable disease course [8, 10]. The molecule is also being investigated as a target for oncolytic viral therapies and monoclonal antibodies due to its specific expression pattern and role in viral entry [7]. However, targeting CD150 carries risks of immunosuppression, as seen in the "immune amnesia" following measles infection where CD150-positive memory cells are depleted [14]. It also acts as a microbial sensor for Gram-negative bacteria, regulating phagosome maturation and autophagy [3, 8]. Its signaling is dependent on adaptor proteins like SAP (SLAM-associated protein), which are critical for proper immune responses [2, 5].

Other names

SLAMSLAMF1IPO-3CDw150

Viral entry receptor for measles virus; homophilic costimulatory receptor for lymphocyte activation