Mannose-binding lectin (MBL) (MBL)

Mannose-binding lectin (MBL) is a key pattern recognition receptor of the innate immune system belonging to the collectin family (UniProt: P11226). It specifically recognizes and binds to terminal carbohydrate motifs, such as D-mannose and L-fucose, which are commonly found on the surfaces of various bacteria, viruses, fungi, and protozoa, as well as on late apoptotic and necrotic host cells (PubMed: 11544344, PubMed: 15128754). Upon binding, MBL activates the lectin complement pathway through its associated serine proteases (MASP-1 and MASP-2), leading to the deposition of C4 and C2 and the formation of C3 convertase (PubMed: 11046020). This process enhances opsonization and direct lysis of pathogens while promoting the non-inflammatory clearance of dying host cells (PubMed: 12615909). MBL deficiency is associated with increased susceptibility to infections, particularly in children and immunocompromised individuals, making recombinant MBL a potential therapeutic candidate for replacement therapy (PubMed: 12443661).

Other names

Mannan-binding lectinMannan-binding proteinMBL2MBPMBP1Collectin-1

MBL acts as a soluble pattern recognition receptor that binds to specific carbohydrate arrays on pathogens and dying host cells, subsequently activating the lectin complement pathway via MASPs to promote opsonization and phagocytosis (PubMed: 11544344).