MASP interactions with plasma-derived MBL.

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

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

Molecular immunology 2012 Sep

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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. Copyright © 2012 Elsevier Ltd. All rights reserved.

Citation

Inga A Laursen, Nicole M Thielens, Michael Christiansen, Gunnar Houen. MASP interactions with plasma-derived MBL. Molecular immunology. 2012 Sep;52(2):79-87