title: F4+ enterotoxigenic Escherichia coli (ETEC) adhesion mediated by the major fimbrial subunit FaeG.
abstract: The FaeG subunit is the major constituent of F4(+) fimbriae, associated with glycoprotein and/or glycolipid receptor recognition and majorly contributes to the pathogen attachment to the host cells. To investigate the key factor involved in the fimbrial binding of F4(+) Escherichia coli, both the recombinant E. coli SE5000 strains carrying the fae operon gene clusters that express the different types of fimbriae in vitro, named as rF4ab, rF4ac, and rF4ad, respectively, corresponding to the fimbrial types F4ab, F4ac, and F4ad, and the three isogenic in-frame faeG gene deletion mutants were constructed. The adhesion assays and adhesion inhibition assays showed that ΔfaeG mutants had a significant reduction in the binding to porcine brush border as well as the intestinal epithelial cell lines, while the complemented strain ΔfaeG/pfaeG restored the adhesion function. The recombinant bacterial strains rF4ab, rF4ac, and rF4ad have the same binding property as wild-type F4(+) E. coli strains do and improvement in terms of binding to porcine brush border and the intestinal epithelial cells, and the adherence was blocked by the monoclonal antibody anti-F4 fimbriae. These data demonstrate that the fimbrial binding of F4(+) E. coli is directly mediated by the major FaeG subunit.
authors.affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China.|Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, China.
authors.forename: Pengpeng
authors.initials: P
authors.lastname: Xia
authors.affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China.|Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, China.
authors.forename: Yujie
authors.initials: Y
authors.lastname: Song
authors.affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China.|Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, China.
authors.forename: Yajie
authors.initials: Y
authors.lastname: Zou
authors.affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China.|Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Yang
authors.affiliation: College of Veterinary Medicine, Yangzhou University, Yangzhou, China.|Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, China.
authors.forename: Guoqiang
authors.initials: G
authors.lastname: Zhu
mesh_terms: D018830:Adhesins, Escherichia coli / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D001422:Bacterial Adhesion; D054307:Enterotoxigenic Escherichia coli / Q000235:genetics / Q000502:physiology*; D004847:Epithelial Cells; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D013552:Swine / Q000382:microbiology
chemical_list: D018830:Adhesins, Escherichia coli; D000911:Antibodies, Monoclonal; C494388:FaeG protein, E coli
keywords: Adherence; F4+ Enterotoxigenic Escherichia coli; FaeG subunit