Title |
Porcine aminopeptidase N binds to F4+ enterotoxigenic Escherichia coli fimbriae
|
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Published in |
Veterinary Research, February 2016
|
DOI | 10.1186/s13567-016-0313-5 |
Pubmed ID | |
Authors |
Pengpeng Xia, Yiting Wang, Congrui Zhu, Yajie Zou, Ying Yang, Wei Liu, Philip R. Hardwidge, Guoqiang Zhu |
Abstract |
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. |
X Demographics
Geographical breakdown
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France | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Canada | 1 | 4% |
Unknown | 25 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 7 | 27% |
Student > Bachelor | 4 | 15% |
Researcher | 3 | 12% |
Other | 2 | 8% |
Student > Master | 2 | 8% |
Other | 2 | 8% |
Unknown | 6 | 23% |
Readers by discipline | Count | As % |
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Veterinary Science and Veterinary Medicine | 7 | 27% |
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Computer Science | 1 | 4% |
Other | 1 | 4% |
Unknown | 9 | 35% |