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. 2019 Mar 19;10:504. doi: 10.3389/fimmu.2019.00504

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Copyright © 2019 Rizk, Maillard, Julian, Knoppova, Green, Novak and Wyatt.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Targets and therapeutic agents of the lectin and alternative complement-activation pathways. (A) The crystal structure of the C4/MASP-2 complex is shown (PDB ID: 4FXG) (149). MASP-2 complement control protein (CCP) domains bind to C4. Upon association with MASP-2, C4 undergoes a conformational change whereby the scissile bond containing R-loop is inserted into the catalytic site of the serine-protease (SP) domain (pale cyan with catalytic triad in magenta). Cleavage yields fragments C4a and C4b. Monoclonal antibody OMS721 binds to a CCP domain of MASP-2, inhibiting the lectin pathway by inhibiting complex formation. (B) The structure of factor B is shown (PDB ID: 2OK5) (150). Upon C3b binding, the N-terminal CCP domains are displaced, leading to rearrangement of the central helices and release of the scissile bond for proteolytic activation. LNP023 inhibits the proteolytic activity of factor B.