MASP interactions with plasma-derived MBL

Inga A Laursen; Nicole M Thielens; Michael Christiansen; Gunnar Houen

doi:10.1016/j.molimm.2012.04.014

MASP interactions with plasma-derived MBL

Mol Immunol. 2012 Sep;52(2):79-87. doi: 10.1016/j.molimm.2012.04.014. Epub 2012 May 18.

Authors

Inga A Laursen¹, Nicole M Thielens, Michael Christiansen, Gunnar Houen

Affiliation

¹ CEA, DSV, Institut de Biologie Structurale (IBS), Grenoble F-38027, France. nicole.thielens@ibs.fr

PMID: 22607836
DOI: 10.1016/j.molimm.2012.04.014

Abstract

The interaction of mannan-binding lectin (MBL) with its associated serine proteases (MASPs) was investigated using recombinant (r) MBL, plasma-derived (pd) MBL, rMASP-3 and rMAp19. When mixed with MBL-deficient serum, rMBL and pdMBL associated with free MASP-2 to (re)gain complement-activating activity. MASPs already associated with pdMBL did not exchange with rMASP-3 or rMAp19, which bound to non-overlapping sites on MBL. Thus, rMASP-3 and rMAp19 bound to free available sites on rMBL and pdMBL. These results have important implications for the therapeutic use of MBL preparations.

MeSH terms

Binding, Competitive
Complement Activation
Humans
In Vitro Techniques
Mannose-Binding Lectin / blood
Mannose-Binding Lectin / metabolism*
Mannose-Binding Protein-Associated Serine Proteases / metabolism*
Multiprotein Complexes / metabolism
Protein Binding
Recombinant Proteins / metabolism

Substances

MBL2 protein, human
Mannose-Binding Lectin
Multiprotein Complexes
Recombinant Proteins
MASP1 protein, human
MASP2 protein, human
Mannose-Binding Protein-Associated Serine Proteases