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. 2014 Aug 22;5:406. doi: 10.3389/fimmu.2014.00406

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Copyright © 2014 Sharp, Whitley, Cunnion and Krishna.

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) or licensor 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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A model of PIC1 interfering with the normal association of C1q/MBL with their cognate serine proteases (C1s–C1r–C1r–C1s/MASPs). Our data suggest PIC1 functionally disrupts the C1s–C1r–C1r– C1s/MASPs interaction with collagen-like region (CLR) of C1q/MBL, respectively. By virtue of PIC1 binding to this region of the CLR, the serine proteases are hypothesized to be in suboptimal conformation for autoactivation and initiation of the classical and/or lectin pathways of complement.