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. 2013 Nov 14;7(Suppl 4):81–89. doi: 10.1111/irv.12197

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© 2013 Blackwell Publishing Ltd

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Alignment of equine IAV M1 sequences. Predicted amino acid sequences of the indicated M1 polypeptides are aligned to a consensus sequence of H3N8 equine M1 polypeptides. A consensus sequence for avian H3N8 M1 proteins is also shown. Residues shown to affect budding morphology in human and/or porcine IAV strains are highlighted by yellow shading. Amino acid differences between the non‐filamentous Miami/63 and consensus sequence are boxed. Cylinders above represent known (solid lines) or predicted (dashed lines) α‐helices in M1 from the N‐terminal (green), middle (ochre) and C‐terminal (grey) domains of the protein.