{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSurfactant protein D (SP‐D), encoded by SFTPD, is a key collectin of the innate immune system that exerts multiple protective functions in the lung and beyond. It recognizes a broad range of pathogen‐associated molecular patterns on bacteria (such as Klebsiella pneumoniae, Pseudomonas aeruginosa, and Helicobacter pylori), viruses (including influenza A and respiratory syncytial virus), fungi, and even endogenous ligands on apoptotic cells. SP‐D promotes aggregation and clearance of these targets—supporting phagocytosis by alveolar macrophages—and modulates inflammatory responses via specific interactions with receptors including toll‐like receptors and LAIR‐1. Through its multimeric structure and its calcium‐dependent carbohydrate recognition domain, SP‐D not only binds microbial saccharides and lipopolysaccharides but also bridges apoptotic and necrotic cells to the clearance machinery, thereby contributing to immune homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic and regulatory studies have revealed that variations in the SFTPD gene affect SP‐D oligomerization, serum levels, and ligand–binding properties, thereby influencing susceptibility to respiratory infections and chronic lung diseases. Several investigations report that specific single‐nucleotide polymorphisms in SFTPD correlate with increased risk or protective profiles in conditions such as severe RSV bronchiolitis, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease, and allergic airway disorders. In parallel, transcriptional regulation (including NFAT‐dependent enhancer activation) and post‐translational modifications directly impact SP‐D expression and function. Furthermore, recombinant fragments of SP‐D (rfhSP‐D) have demonstrated anti‐infective and anti‐allergic activity in animal models, underscoring its potential as both a therapeutic agent and biomarker in pulmonary diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its direct antimicrobial activities, SP‐D functionally interacts with other innate immune molecules and mediators. It cooperates with proteins such as SP‐A, human neutrophil defensins, and even mucin or pharmacologic inhibitors (e.g., oseltamivir) to modulate viral neutralization and inflammatory cell activation. SP‐D is itself subject to proteolytic degradation by microbial enzymes (for example, P. aeruginosa elastase and dust mite proteases), which can impair its function and influence disease pathogenesis in conditions such as cystic fibrosis and allergic asthma. Moreover, SP‐D is expressed extra‐pulmonarily, for instance in the nasal mucosa, and its levels in serum or bronchoalveolar lavage fluid serve as valuable biomarkers for the diagnosis and prognosis of a range of pulmonary disorders, including severe asthma, obstructive sleep apnea, and systemic sclerosis–related interstitial lung disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "39", "end_ref": "44"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Emma Murray, Wafa Khamri, Marjorie M Walker, et al. 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