{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nToll‐like receptor 2 (TLR2) is a key pattern‐recognition receptor whose extracellular leucine‐rich repeat domain forms an “m‐shaped” structure upon ligand binding. TLR2 heterodimerizes with TLR1 or TLR6—processes elucidated by high‐resolution crystal studies—that expand its ligand spectrum to include tri‐acylated and di‐acylated lipopeptides, among other microbial components. In addition, TLR2 clusters within membrane lipid rafts and cooperates with accessory molecules to fine‐tune ligand recognition and downstream signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTLR2 serves as an essential sensor not only for microbial products but also for endogenous “danger‐associated” molecules. Activation of TLR2 by bacterial cell wall components such as lipoteichoic acids or lipopeptides leads to antimicrobial responses—exemplified by vitamin D–mediated cathelicidin induction in macrophages—and it is also engaged by host‐derived proteins including heat‐shock protein 70, high-mobility group box 1, histones, and alpha-synuclein. These ligands differentially trigger TLR2–mediated signaling cascades, often via MyD88 and NF-κB, resulting in specific cytokine profiles that can favor either a Th1 or Th2 immune outcome. In some instances, TLR2 function is modulated by accessory receptors such as CD14, and genetic variations (e.g. Arg753Gln) in the TLR2 gene further influence ligand responsiveness and susceptibility to bacterial infections."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in recognizing molecular patterns, TLR2 is a central mediator in diverse host–pathogen interactions and in the modulation of inflammatory responses. TLR2 activation has been implicated in the sensing of viral glycoproteins—including measles virus and SARS‐CoV‐2 envelope proteins—as well as fungal molecules, contributing to cytokine production in different disease settings such as tuberculosis, septic shock, and invasive aspergillosis. Moreover, TLR2 functions as a costimulatory receptor on T cells, influences innate responses in metabolic disorders like type 1 and type 2 diabetes, and is modulated by dietary fatty acids. Genetic polymorphisms and age‐associated alterations in TLR1/2 expression further affect cytokine responses, while TLR2 signaling can be subverted by pathogens such as Porphyromonas gingivalis to uncouple phagocytosis from inflammation. Other studies have revealed that TLR2 engagement by endogenous ligands—including eosinophil-derived neurotoxin and free fatty acids—can amplify proinflammatory cascades, thereby bridging innate immunity with adaptive responses and contributing to disease pathogenesis in conditions such as neurodegeneration, atherosclerosis, and islet inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Matthew A Worsley, Nick M Clayton, Chas Bountra, et al. 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