MASP interactions with plasma-derived MBL

► MASPs bind to MBL in a non-exchangeable manner. ► MASPs bind to free sites on plasma MBL. ► MASP-3 and MAp19 have non-overlapping binding sites on MBL. ► MASP-depleted plasma MBL and recombinant MBL regain complement-activating ability when mixed with MASP-2 containing serum. The interaction of ma...

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Bibliographic Details
Published in:Molecular immunology 2012-09, Vol.52 (2), p.79-87
Main Authors: Laursen, Inga A., Thielens, Nicole M., Christiansen, Michael, Houen, Gunnar
Format: Article
Language:English
Subjects:
Binding, Competitive
Complement Activation
Exchange
Humans
In Vitro Techniques
Mannose-Binding Lectin - blood
Mannose-Binding Lectin - metabolism
Mannose-Binding Protein-Associated Serine Proteases - metabolism
MASP
MBL
Multiprotein Complexes - metabolism
Plasma
Protein Binding
Recombinant protein
Recombinant Proteins - metabolism
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Summary:► MASPs bind to MBL in a non-exchangeable manner. ► MASPs bind to free sites on plasma MBL. ► MASP-3 and MAp19 have non-overlapping binding sites on MBL. ► MASP-depleted plasma MBL and recombinant MBL regain complement-activating ability when mixed with MASP-2 containing serum. 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.
ISSN:0161-5890
1872-9142
DOI:10.1016/j.molimm.2012.04.014