MASP2 (protein)

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Mannan-binding lectin serine protease 2 also known as mannose-binding protein-associated serine protease 2 (MASP-2) is an enzyme that in humans is encoded by the MASP2 gene.[1][2][3]


The Ra-reactive factor (RARF) is a complement-dependent bactericidal factor that binds to the Ra and R2 polysaccharides expressed by certain enterobacteria. Alternate splicing of this gene results in two transcript variants encoding two RARF components that are involved in the mannan-binding lectin pathway of complement activation. The longer isoform is cleaved into two chains which form a heterodimer linked by a disulfide bond. The encoded proteins are members of the trypsin family of peptidases.[1]

MASP-2 is involved in the complement system. MASP-2 is very similar to the C1s molecule, of the classical complement pathway, and they are thought to have a common evolutionary ancestor. When the carbohydrate-recognising heads of MBL bind to specifically arranged mannose residues on the surface of a pathogen, MASP-2 is activated to cleave complement components C4 and C2 into C4a, C4b, C2a, and C2b.

See also


  1. 1.0 1.1 "Entrez Gene: mannan-binding lectin serine peptidase 2". 
  2. Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen SB, Poulsen K, Willis AC, Eggleton P, Hansen S, Holmskov U, Reid KB, Jensenius JC (April 1997). "A second serine protease associated with mannan-binding lectin that activates complement". Nature. 386 (6624): 506–10. Bibcode:1997Natur.386..506T. PMID 9087411. doi:10.1038/386506a0. 
  3. Vorup-Jensen T, Jensenius JC, Thiel S (August 1998). "MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway". Immunobiology. 199 (2): 348–57. PMID 9777418. doi:10.1016/S0171-2985(98)80039-9. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain. Template:PDB Gallery

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