Binding determinants in the interplay between porcine aminopeptidase N and enterotoxigenic &ITEscherichia coli&IT F4 fimbriae

文献类型： 外文期刊

第一作者： Xia, Pengpeng

作者： Xia, Pengpeng;Quan, Guomei;Yang, Yi;Zhao, Jing;Wang, Yiting;Zhou, Mingxu;Zhu, Jianzhong;Zhu, Guoqiang;Xia, Pengpeng;Quan, Guomei;Yang, Yi;Zhao, Jing;Wang, Yiting;Zhou, Mingxu;Zhu, Jianzhong;Zhu, Guoqiang;Liu, Siguo;Hardwidge, Philip R.;Xia, Pengpeng;Quan, Guomei;Yang, Yi;Zhao, Jing;Zhu, Guoqiang

作者机构：

期刊名称：VETERINARY RESEARCH （ 影响因子：3.683； 五年影响因子：4.106 ）

ISSN： 0928-4249

年卷期： 2018 年 49 卷

页码：

收录情况： SCI

摘要： The binding of F4(+) enterotoxigenic Escherichia coil (ETEC) and the specific receptor on porcine intestinal epithelial cells is the initial step in F4(+) ETEC infection. Porcine aminopeptidase N (APN) is a newly discovered receptor for F4 fimbriae that binds directly to FaeG adhesin, which is the major subunit of the F4 fimbriae variants F4ab, F4ac, and F4ad. We used overlapping peptide assays to map the APN-FaeG binding sites, which has facilitated in the identifying the APN-binding amino acids that are located in the same region of FaeG variants, thereby limiting the major binding regions of APN to 13 peptides. To determine the core sequence motif, a panel of FaeG peptides with point mutations and FaeG mutants were constructed. Pull-down and binding reactivity assays using piglet intestines determined that the amino acids G159 of F4ab, N209 and L212 of F4ac, and A200 of F4ad were the critical residues for APN binding of FaeG. We further show using ELISA and confocal microscopy assay that amino acids 553-568, and 652-670 of the APN comprise the linear epitope for FaeG binding in all three F4 fimbriae variants.

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