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. 2018 Jul 26;8:11250. doi: 10.1038/s41598-018-29258-0

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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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Working hypothesis. (a) FUT2^−/− individuals or children (<2 years old) express Le^a on type 1 O-linked glycans of the small intestinal mucosa. We have evidence to suggest they are susceptible to symptomatic ETEC CFA/I (and related CFA/I CF family members) infection. FUT2^+/+ or FUT2^+/− individuals (>2 years old) express Le^b on type 1 O-linked glycans of the small intestinal mucosa. We have not found these individuals to not be susceptible to ETEC CFA/I (and related CFA/I CF family members) infection. (b) ETEC CFA/I fimbriae contains >1,000 copies of a major subunit (CfaB), with one or a few copies of the tip residing minor subunit (CfaE). A 12-aa stretch V²⁴EKNITVTASVD³⁵ of the Ig-like binding groove region of CfaB served as a CFA/I docking site our in-silico docking analysis. This 12 amino acid stretch also shares structural similarities with all ETEC CF major subunits of the CFA/I CF like family, and with class 1 pili from bacteria that can cause urinary and respiratory infections by binding to host glycolipids containing HBGAs. (c) Using our small intestinal like glycan defined CHO-K1 cell lines, we have demonstrated that CfaB of ETEC CFA/I fimbriae, as well as four related CFs, bind more to our CHO-K1 cell-line expressing Le^a, compared to cells carrying Le^b or the CHO-K1 wild-type glycan phenotype. Using in-silico docking analysis, we predict up to three amino acids (Glu²⁵, Asn²⁷, Thr²⁹) found in the immunoglobulin (Ig)-like groove region of CfaB of CFA/I and related CF fimbriae, could be important for the preferential and higher affinity binding of CFA/I fimbriae to Le^a glycans. These findings may lead to a better molecular understanding of ETEC pathogenesis, aiding in the development of vaccines and/or anti-infection therapeutics, which block such host-pathogen interactions.