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. 2014 Sep 22;7:443. doi: 10.1186/1756-3305-7-443

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© Rieille et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Locations of the mutations in the Envelope protein of TBEV are shown. (A) Left, top: the primary structure of the TBEV envelope protein and its organization into the ectodomain, stem, and trans-membrane (TM) region. The region encompassing amino acid residues 249-496 (indicated by “>” and “<”) corresponds to the terminal part of the envelope gene that was sequenced in this study. All non-synonymous substitutions in the partial sequences of the Canton Valais TBEV isolates mapped to the stem region of the Envelope protein. (A) Left, bottom: Alignment of the Envelope protein amino acid sequences of the 21 Canton Valais TBEV isolates reported in this study and two reference sequences (Raron_HM468176 and Salgesch_HM468177). Amino acid substitutions were found at positions 416, 437, 439, 440, 444 and 447. Right: the three-dimensional structure of a single TBEV E molecule based on the homology model of the dengue virus E molecule (PDB 3 J27). The N-terminal ectodomain is attached to the stem and consists of three domains: central domain (D1; in red), the fusion domain (D11; in yellow), and the lateral domain (DIII; in blue). The stem consists of three helices (H1, H2, and H3; in magenta) and the side chains of the amino acid substitutions are shown (pink spheres). The two trans-membrane helices (T1 and T2; in gray) are inserted in the viral membrane. (B) Close-up of the variable residues in the H3 helix of the stem. The mutated residues are labeled. (C) Close-up of the mutant I416 residue, which projects into a hydrophobic pocket (residues lining this pocket are displayed as sticks).