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Porcine aminopeptidase N binds to F4+ enterotoxigenic Escherichia coli fimbriae
- Xia, Pengpeng, Wang, Yiting, Zhu, Congrui, Zou, Yajie, Yang, Ying, Liu, Wei, Hardwidge, Philip R., Zhu, Guoqiang
- Veterinary research 2016 v.47 no.1 pp. 24
- antibodies, diarrhea, enterotoxigenic Escherichia coli, fimbriae, gene expression, intestinal mucosa, membrane alanyl aminopeptidase, piglets, receptors, serotypes, two hybrid system techniques
- F4⁺ enterotoxigenic Escherichia coli (ETEC) strains cause diarrheal disease in neonatal and post-weaned piglets. Several different host receptors for F4 fimbriae have been described, with porcine aminopeptidase N (APN) reported most recently. The FaeG subunit is essential for the binding of the three F4 variants to host cells. Here we show in both yeast two-hybrid and pulldown assays that APN binds directly to FaeG, the major subunit of F4 fimbriae, from three serotypes of F4⁺ ETEC. Modulating APN gene expression in IPEC-J2 cells affected ETEC adherence. Antibodies raised against APN or F4 fimbriae both reduced ETEC adherence. Thus, APN mediates the attachment of F4⁺ E. coli to intestinal epithelial cells.