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. 2020 Dec 14;11:568631. doi: 10.3389/fimmu.2020.568631

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Copyright © 2020 Najafpour, Cardoso, Canário and Power

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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Comparison of the fish and human C3 thioester bond. (A) Schematic representation of the thirteen conserved domains of human C3. (B) Sequence comparison of the fish, human and chicken C3 thioester bond responsible for attaching the complement proteins to the surface of the pathogen. The six aa motif forming the thioester bond are colored and conserved aa are denoted in the same color. The C3.1 (red) and C3.2 (pink) sequences were grouped to better illustrate the differences within this region. SP, signal peptide; MG, macroglobulin domain (1-8); LNK, link domain; ANATO, anaphylatoxin domain; α-NT, N-terminal region of the cleaved α-chain; CUB, complement C1r/C1s, Uegf, Bmp1 domain; TED, thioester-containing domain; SAR, short anchor region; C345C, carboxy-terminal domain.