{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSiglec‐7 is a member of the CD33‐related sialic acid–binding immunoglobulin‐like lectin family that is predominantly expressed on natural killer (NK) cells, monocytes, and certain T‐cell subsets. Structural studies have revealed that Siglec‐7 possesses a specialized V‐set domain with a uniquely configured ligand‐binding pocket that preferentially recognizes α2,8‐linked disialic acids. Its intracellular domain contains immunoreceptor tyrosine‐based inhibitory motifs (ITIMs) that, upon ligand engagement, recruit phosphatases such as SHP-1 and SHP-2 to attenuate activating signals. Mutagenesis and high-resolution crystallography have identified critical amino acids—in the primary binding site (e.g., R124) and in a secondary region (including R67 and the newly recognized conserved R94)—as essential for optimal sialic acid recognition and inhibitory function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFunctionally, Siglec‐7 operates as an immune checkpoint receptor by negatively regulating NK cell cytotoxicity and modulating T‐cell receptor signaling. Alterations in its surface expression have been linked to multiple disease states. In certain cancers, malignant cells display aberrant sialoglycosylation that engages Siglec‐7, thereby dampening NK cell–mediated cytotoxicity—even though loss of Siglec‐7 expression may correlate with enhanced killing in some leukemia models. In viral infections such as HIV, reduced Siglec‐7 levels on NK cells are an early indicator of immune dysregulation, while in hepatocellular carcinoma and other pathologies, diminished Siglec‐7 expression is associated with impaired activating receptor profiles. Moreover, epigenetic modifications can regulate Siglec‐7 expression, underscoring its potential utility both as a biomarker and as a therapeutic target in cancer immunotherapy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these classical inhibitory roles, Siglec‐7 contributes to a broader spectrum of immune regulation. Its interactions with ligands such as disialyl core 1 O‐glycans and the mucin‐type glycoprotein CD43 have been implicated in the formation of glyco–immune checkpoints that govern T‐cell activation. Siglec‐7 also mediates responses in infectious diseases—for example, by binding varicella–zoster virus glycoprotein B to facilitate infection of hematopoietic cells—and plays roles in modulating inflammatory cytokine production in monocytes upon receptor crosslinking. Furthermore, novel applications include the engineering of Siglec‐7–based chimeric antigen receptors to redirect T‐cell cytotoxicity, its involvement in placental immune tolerance via interactions with glycodelin-A, and even regulation of platelet apoptosis. Together, these diverse functions establish Siglec‐7 as a multifaceted immunoregulatory receptor with promising potential for therapeutic intervention in cancer, infectious, and metabolic disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Magnus S Alphey, Helen Attrill, Paul R Crocker, et al. 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