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. 2018 May 30;8:8390. doi: 10.1038/s41598-018-26570-7

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© The Author(s) 2018

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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(a) Blast alignments of V. cholerae AcfC with similar proteins from enteropathogenic bacteria (Paa from E. coli and PEB3 from C. jejuni) using Clustal W software; (b) Detection of V. cholerae AcfC expression in the different bacterial cell compartments using anti-AcfC antibodies. M: Page ruler plus pre-stained protein ladder (Thermo Fisher Scientific); S: Supernatant fraction; OM: Outer membrane fraction; P: Periplasmic fraction; IM: Inner membrane fraction; C: Cytoplasmic fraction; Ctrl: Ni-NTA purified His₆-tagged AcfC, used as a positive control; (c) ELISA analysis of binding AcfC to different sulfated glycosaminoglycans (heparin sulfate and chondroitin sulfate), non-sufated glycosaminoglycan (hyaluronic acid) and type II porcine mucin. The values are the means ± standard deviation (n = 3). *p < 0.05, as determined by Tukey’s test.