Characterization of the adhesin of Escherichia coli F18 fimbriae.
Previous research has suggested that the adhesin encoded by the F18 fimbrial operon in Escherichia coli is either the FedE or FedF protein. In this work, we show that anti-FedF antibodies, unlike anti-FedE serum, were able to inhibit E. coli adhesion to porcine enterocytes. Moreover, specific adhesion to enterocytes was shown with purified FedF-maltose binding protein.
Smeds
A
A
Faculty of Veterinary Medicine, Department of Basic Veterinary Sciences, Section of Microbiology, 00014 University of Helsinki, Finland.
Hemmann
K
K
Jakava-Viljanen
M
M
Pelkonen
S
S
Imberechts
H
H
Palva
A
A
D018829:Adhesins, Bacterial; D000818:Animals; D000907:Antibodies, Bacterial; D001422:Bacterial Adhesion; D003001:Cloning, Molecular; D020895:Enterocytes / Q000382:microbiology; D004926:Escherichia coli / Q000235:genetics / Q000472:pathogenicity*; D029968:Escherichia coli Proteins / Q000276:immunology / Q000502:physiology*; D010861:Fimbriae, Bacterial / Q000737:chemistry* / Q000235:genetics; D019084:Fluorescent Antibody Technique, Indirect; D007082:Ileum / Q000166:cytology / Q000382:microbiology; D007583:Jejunum / Q000166:cytology / Q000382:microbiology; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins; D013552:Swine
D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; D029968:Escherichia coli Proteins; C440653:FedF protein, E coli; D011993:Recombinant Fusion Proteins