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Pathogen-associated carbohydrate moieties recognized by surfactant protein D (SP-D) represent a diverse class of microbial surface molecules, including lipopolysaccharides (LPS), lipoteichoic acids (LTA), and various terminal glycans. These moieties serve as pathogen-associated molecular patterns (PAMPs) that are specifically identified by the C-type lectin domain of SP-D, a key component of the innate immune system (Nayak et al., 2012, PMID: 22703241). Upon binding, SP-D facilitates the aggregation, opsonization, and subsequent clearance of pathogens such as bacteria, viruses, and fungi by alveolar macrophages (Watson et al., 2019, PMID: 31110321). In addition to direct antimicrobial activity, the interaction between SP-D and these carbohydrate targets modulates inflammatory signaling pathways, helping to maintain pulmonary homeostasis (Gardai et al., 2003, PMID: 14560035). Therapeutic strategies often involve the use of recombinant human SP-D or its fragments to target these moieties in conditions like neonatal respiratory distress syndrome, chronic obstructive pulmonary disease (COPD), and various respiratory infections (UniProt P35247).
Binding to terminal sugars (e.g., mannose, fucose, glucose) on pathogen surfaces via the C-terminal carbohydrate recognition domain (CRD) in a calcium-dependent manner, leading to pathogen neutralization and enhanced phagocytosis.
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