The SLAMF1 gene is located on human chromosome 1 and consists of eight exons and seven introns . The gene undergoes alternative splicing, resulting in several isoforms of the protein, including the conventional transmembrane isoform (mCD150), secreted isoform (sCD150), cytoplasmic isoform (cCD150), and the novel transmembrane isoform (nCD150) .
SLAMF1 is a type I transmembrane protein with a molecular weight between 70 kDa and 95 kDa . The extracellular region of the receptor comprises one Ig variable-like domain and one Ig constant 2-like domain . The intracellular region contains two intracellular tyrosine-based switch motifs (ITSMs) that interact with SH2 domain-containing proteins . However, the nCD150 isoform lacks ITSMs, and the sCD150 isoform lacks the transmembrane domain, preventing it from anchoring to the cell membrane .
SLAMF1 is expressed in various hematopoietic cells, including thymocytes, NKT cells, T cells, B cells, monocytes, macrophages, and dendritic cells . Its expression is upregulated upon activation of these cells . Additionally, SLAMF1 is used as a marker for identifying hematopoietic stem cells . The expression of SLAMF1 is regulated by factors such as Early B-cell factor 1 (EBF1), STAT6, IRF4, and NF-kB, which are involved in signal transduction from the B-cell receptor, its co-receptors, and IL-4R .
SLAMF1 plays a significant role in the immune response by regulating macrophages’ phagosomal functions and promoting Th1-protective responses . It acts as a self-ligand receptor that can internalize gram-negative bacteria and regulate macrophages’ phagosomal functions . In the context of tuberculosis, SLAMF1 enhances the uptake of Mycobacterium tuberculosis by human monocyte-derived macrophages and participates in the endolysosomal maturation process .