Ontology highlight
ABSTRACT:
SUBMITTER: Xia P
PROVIDER: S-EPMC5828407 | biostudies-literature | 2018 Feb
REPOSITORIES: biostudies-literature
Xia Pengpeng P Quan Guomei G Yang Yi Y Zhao Jing J Wang Yiting Y Zhou Mingxu M Hardwidge Philip R PR Zhu Jianzhong J Liu Siguo S Zhu Guoqiang G
Veterinary research 20180226 1
The binding of F4<sup>+</sup> enterotoxigenic Escherichia coli (ETEC) and the specific receptor on porcine intestinal epithelial cells is the initial step in F4<sup>+</sup> 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- ...[more]