Mannose-binding lectin pathway components (MBL)

The **mannose-binding lectin pathway components** are a group of proteins central to the lectin pathway of the complement system, a major mechanism of innate immunity. The principal protein, **Mannose-binding lectin (MBL)**, is a liver-derived collectin that recognizes specific carbohydrate patterns on the surfaces of diverse pathogens. Upon binding, MBL associates with serine proteases (MASPs), initiating a proteolytic cascade resulting in complement activation, opsonization, phagocytosis, and microorganism elimination[1][3][5]. Deficiencies or dysregulation of these components can predispose to infections, inflammation, and various diseases including cancer and cardiovascular conditions[2][6][8]. MASP-2, a serine protease associated with MBL, is an active target of emerging therapeutics aiming to selectively modulate the lectin complement pathway for the treatment of rare and common diseases[4][6]. Current therapeutic and diagnostic strategies focus on modulating the activity or levels of MBL/ficolins/MASPs, or on their genetic regulation, highlighting their broad relevance in immunology and medicine.

Other names

Mannan-binding lectinMannan-binding proteinMannose-binding proteinMBL2 (gene encoding MBL)MASP-2 (for the serine protease)

Inhibition of MASP-2 blocks lectin pathway activation, reducing downstream complement activation, inflammation, and tissue injury. Anti-MBL approaches reduce complement-mediated damage; e.g., in ischemic stroke. Modulation of MBL2 expression (e.g., via miRNAs) to alter cancer cell proliferation/metastasis.