title: MASP interactions with plasma-derived MBL.
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.
authors.affiliation: CEA, DSV, Institut de Biologie Structurale (IBS), Grenoble F-38027, France. nicole.thielens@ibs.fr
authors.forename: Inga A
authors.initials: IA
authors.lastname: Laursen
authors.forename: Nicole M
authors.initials: NM
authors.lastname: Thielens
authors.forename: Michael
authors.initials: M
authors.lastname: Christiansen
authors.forename: Gunnar
authors.initials: G
authors.lastname: Houen
mesh_terms: D001667:Binding, Competitive; D003167:Complement Activation; D006801:Humans; D066298:In Vitro Techniques; D037601:Mannose-Binding Lectin / Q000097:blood / Q000378:metabolism*; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: C445619:MBL2 protein, human; D037601:Mannose-Binding Lectin; D046912:Multiprotein Complexes; D011994:Recombinant Proteins; C084067:MASP1 protein, human; C105296:MASP2 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases