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. 2020 Nov 5;12(11):1258. doi: 10.3390/v12111258

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Structural features of rEDI^ZIKALIVax. Tridimensional structure prediction of rEDI ^ZIKALIVax and its mutants was performed by comparative modeling on PHYRE² protein recognition server (http://www.sbg.bio.ic.ac.uk/~phyre2/html/page.cgi?id=index). The predicted structures were analyzed with Chimera, a program for interactive visualization of tridimensional molecules. In (A), predicted structure of ZIKALIVax rEDI with GL region in green. The two C-terminal tags of rEDI are not presented. In (B,C), the ZIKALIVax GL region structure (GL^ZIKALIVax) was compared to GL mutants bearing the two mutations E-T152I, and E-I156T (B) or the three mutations E-T152I, E-I156T, and E-Y158H (C). The hatched arrow indicates the position of residue I152 in the 3D structure of GL mutant.