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. 2015 Oct 5;12:155. doi: 10.1186/s12985-015-0394-1

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© Anoh et al. 2015

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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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Fig. 1 — a Map of the study area in Western Côte d’Ivoire showing the sampling localities in the red circle. Villages are represented by black dots, the boundary of Taï National park by green line, road by black line, tracks by purple lines, rivers by blue lines. b Alignment of partial glycoprotein B amino acid (aa) sequences shown as a cartoon. Conserved aa are given in grey color; non-conserved aa are colored according to their type. The region between aa positions 190 and 230 comprises the recognition motif for the cellular endoprotease furin. For the HCMV strains, their cleavage site (CLS) type is indicated by numbers (CLS1-CLS5). The study sequence names are marked with a star