Mannan-binding lectin (MBL), encoded by the *MBL2* gene, is a key pattern-recognition molecule in the innate immune system. Produced primarily in the liver, MBL belongs to the collectin family and binds to carbohydrate structures (e.g., mannose, N-acetylglucosamine) on pathogens like bacteria, viruses, and fungi. This binding activates the lectin complement pathway via MBL-associated serine proteases (MASPs), promoting opsonization, inflammation, and pathogen clearance.
*MBL2* polymorphisms significantly influence serum MBL levels and functional activity. Variants in the promoter region and exon 1 (e.g., codons 52. 54. 57) are linked to MBL deficiency, affecting 5-30% of populations. Low MBL is associated with increased susceptibility to infections (especially in immunocompromised individuals) and autoimmune or inflammatory disorders, though its clinical impact varies with genetic and environmental factors.
Anti-MBL antibodies, either monoclonal or polyclonal, are essential tools for research and diagnostics. They enable quantification of MBL in serum, tissue localization studies, and functional assays to assess complement activation. In clinical settings, these antibodies help identify MBL deficiency or dysregulation, guiding therapeutic strategies (e.g., recombinant MBL replacement). However, challenges remain in standardizing assays and interpreting MBL’s complex role in disease pathogenesis.