MASP interactions with plasma-derived MBL
Copyright policy )MASP interactions with plasma-derived MBL
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.
- Joseph Fourier University France
- Institut de Biologie Structurale France
- Statens Serum Institut Denmark
- Grenoble Alpes University France
- French National Centre for Scientific Research France
Mannose-Binding Protein-Associated Serine Proteases, Multiprotein Complexes, Humans, In Vitro Techniques, Binding, Competitive, Complement Activation, Mannose-Binding Lectin, Recombinant Proteins, Protein Binding
Mannose-Binding Protein-Associated Serine Proteases, Multiprotein Complexes, Humans, In Vitro Techniques, Binding, Competitive, Complement Activation, Mannose-Binding Lectin, Recombinant Proteins, Protein Binding
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