Mannose-binding protein C (MBL2) (MBL2)

Mannose-binding protein C, commonly known as Mannose-binding lectin (MBL), is a soluble pattern recognition receptor that plays a pivotal role in the innate immune system (UniProt P11226). It belongs to the collectin family and is characterized by its ability to bind to specific carbohydrate arrays, such as mannose and N-acetylglucosamine, found on the surfaces of diverse pathogens including bacteria, viruses, and fungi (PMID: 11748273). Once bound, MBL triggers the lectin pathway of the complement system by activating MBL-associated serine proteases (MASPs), which facilitates pathogen opsonization, phagocytosis, and direct lysis (PMID: 12615312). Genetic polymorphisms in the MBL2 gene frequently result in MBL deficiency, a condition linked to increased susceptibility to infections, particularly in children and immunocompromised patients (NCBI Gene: 4153). Beyond its role in infection, MBL is implicated in the clearance of apoptotic cells and the modulation of inflammatory responses, though its over-activation can contribute to tissue injury in ischemia-reperfusion scenarios (PMID: 21172303). Therapeutic interventions focus on MBL replacement therapy using recombinant or plasma-derived MBL to treat deficiency, while inhibitors of the lectin pathway are being investigated to mitigate complement-mediated damage in acute inflammatory conditions (PMID: 18510743).

Other names

Mannose-binding lectinMannan-binding lectinMannan-binding proteinMBPMBP-CMBLSoluble mannose-binding lectin

Restoration of the lectin complement pathway through replacement therapy in deficient individuals; binding to pathogen-associated molecular patterns (PAMPs) to initiate opsonization and complement-mediated lysis.