{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPGLYRP1 is an innate immunity protein that functions as a pattern‐recognition receptor for bacterial peptidoglycan. In several studies, PGLYRP1 (often known as Tag7 or PGRP‐S) has been shown to bind directly to bacterial cell wall components, thereby inhibiting bacterial growth and even mediating direct bactericidal effects. For example, one study demonstrated that PGLYRP1 binds peptidoglycan on both Gram‐positive and Gram‐negative bacteria, exhibiting antimicrobial activity that is potentiated by synergy with lysozyme, while another work showed that recombinant PGLYRP1 interacts with Borrelia burgdorferi peptidoglycan to kill the spirochete. In addition, targeted activation of endogenous PGLYRP genes in cell lines using genome‐editing strategies was found to inhibit the development of infections such as those caused by Chlamydia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn parallel, PGLYRP1 serves as a ligand or co–ligand for receptors that drive inflammatory and cytotoxic responses. Several reports have revealed that PGLYRP1 can form stable complexes with molecules such as Hsp70, and—in a soluble or multimeric form—act as an agonist of the triggering receptor expressed on myeloid cells‐1 (TREM‐1). These interactions promote downstream proinflammatory signaling and activate cytotoxic lymphocyte populations (including natural killer cells and T lymphocytes) that mediate tumor cell lysis via apoptotic and necroptotic mechanisms. Moreover, a short peptide derived from PGLYRP1 has been shown to recapitulate TREM‐1 activation, thus highlighting its versatile role in amplifying innate immune responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "11"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its antimicrobial and proinflammatory functions, PGLYRP1 also participates in the regulation of immune cell behavior through its interactions with additional accessory proteins. Complex formation between PGLYRP1 and proteins such as S100A4 (Mts1) can drive the chemotactic migration of lymphocytes, while binding to HspBP1 modulates the formation and cytotoxic potential of PGLYRP1–Hsp70 complexes. Furthermore, expression of PGLYRP1 in specialized mucosal and antigen‐sampling cells (for example, M cells) underscores its role in orchestrating immune surveillance at epithelial surfaces."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "16"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinical and genetic studies have further linked dysregulation of PGLYRP1 to several inflammatory and immune‐related disorders. Altered expression or polymorphisms in the genes encoding PGLYRP1 have been associated with psoriasis, rheumatoid arthritis, and periodontitis, while elevated serum or salivary levels of PGLYRP1 serve as potential biomarkers for coronary artery disease, heart failure, and periodontal as well as neuroinflammatory conditions. Moreover, altered PGLYRP1 expression in epithelial cells has been observed in the context of esophageal cancer, underscoring its multifaceted role in disease states and highlighting its promise as both a diagnostic marker and a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "29"}]}, {"type": "t", "text": ""}]}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ju Hyun Cho, Iain P Fraser, Koichi Fukase, et al. 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