{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMBL2 encodes mannose‐binding lectin (MBL), a key soluble pattern‐recognition molecule of innate immunity. MBL recognizes specific carbohydrate structures on the surfaces of a wide range of pathogens—including bacteria, viruses, and fungi—and, upon binding, triggers the lectin pathway of complement activation via its associated serine proteases. This activation leads to opsonization, enhanced phagocytosis, and modulation of inflammatory responses. In addition, proper higher‐order oligomerization of MBL is critical for optimal ligand binding and complement activation, and naturally occurring mutations in MBL2 can compromise these functions."}, {"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": "\nIn numerous clinical and epidemiological studies, genetic polymorphisms within MBL2 have been shown to influence serum levels and functional activity of MBL, thereby affecting host susceptibility to infectious agents and inflammatory insults. Low‐producing variant alleles correlate with impaired complement activation and have been linked to increased risks for common childhood infections, invasive pneumococcal disease, severe acute respiratory syndrome (SARS), sepsis, and even tuberculosis. Moreover, altered MBL levels—whether due to genetic differences or environmental modulation—appear to modify disease course not only in infectious diseases but also in immune‐mediated conditions and following procedures such as transplantation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its traditional role in microbial recognition and complement-mediated clearance, MBL also plays multifaceted roles in other clinical contexts. Elevated or aberrant MBL-mediated complement activation has been implicated in contributing to tissue injury in conditions such as diabetic vascular complications, trauma-induced “complementopathy,” and even in the tumor microenvironment where binding to altered glycans may amplify inflammatory signals and oncogenic progression (for example, in pancreatic ductal adenocarcinoma). In transplantation and other immunocompromised states, variations in MBL levels further influence the risk of rejection and post-transplant infection. In some settings, low MBL levels may afford partial protection against intracellular pathogens, illustrating the context-dependent nature of its function. Overall, the interplay between MBL2 genetic variants, serum MBL concentration, and its ability to activate complement underscores its central role in bridging innate immunity with both host defense and inflammatory pathology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "A Koch, M Melbye, P Sørensen, et al. 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