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. 2017 Sep 21;7:12075. doi: 10.1038/s41598-017-12458-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Characterization of the AT12-015 mAb resistant (MAR) HPeV3 variant. (a) Nonlinear regression analysis of the neutralizing activity of a human AT12-015 mAb against the HPeV3 A308/99 wild-type (wt) and the MAR HPeV3 variant. Data presented as the mean ± SD. (b) Immunofluorescence imaging of HPeV3 A308/99 wt and MAR variant infected HT29 cells stained by a rabbit HPeV1 antiserum (HPeV1 pAb) or the AT12-015 mAb. (c) Amino acid mutations in the MAR HPeV3 variant as compared to the A308/99 wt and the clinical isolates. Capsid surface-exposed residues are highlighted in red. (d) HPeV3 roadmap of capsid exterior. Capsid proteins VP0 (blue), VP3 (green) and VP1 (pink), the AT12-015 Fab footprint (yellow contour), and also amino acid mutations in variant resistant to AT12-015 are shown (red).