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. 2018 Jul 26;9:1683. doi: 10.3389/fimmu.2018.01683

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Copyright © 2018 Wang, Hu, Wangkahart, Liu, Wang, Zahran, Maisey, Liu, Xu, Imarai and Secombes.

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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Amino acid (aa) sequence alignment of IL-2 mature peptides from salmonids and selected fish and mammalian species (A) and predicted potential intra-molecular disulfide bonds (B). (A) The multiple alignment was produced using ClustalW, and conserved aa shaded using BOXSHADE (version 3.21). The four α helices (A–D) are indicated above the alignment. The conserved cysteine residues are in red and numbered at the bottom of the alignment (C1–8). The aa sequences and accession numbers are detailed in Supplementary Material: protein sequences. (B) Lineage- and paralog-specific conservation of cysteine residues in mammalian IL-2, salmonid IL-2A and other fish IL-2, and salmonid IL-2B and IL-2L is apparent. Cysteine residues potentially forming disulfide bonds are linked by green lines.