Cloning and characterization of the eae gene from a dog attaching and effacing Escherichia coli strain 4221
1997
An, H. | Fairbrother, J.M. | Dubreuil, J.D. | Harel, J.
We have cloned and determined the nucleotide sequence of the eae gene from a dog attaching and effacing (A/E) Escherichia coli (DEPEC) strain 4221. When comparing the predicted amino acid sequence of the eae(DEPEC) to that of the Eae proteins from enteropathogenic E. coli (EPEC), enterohaemorrhagic E coli O157:H7 (EHEC), Citrobacrer freundii biotype 4280, and a swine A/E E. coli strain O45 (PEPEC), the overall sequence identity was 84, 81, 83 and 83%, respectively, with the greatest divergence at the C-terminal end, the putative receptor-binding portion. Interestingly, the DEPEC Eae shares the greatest identity at the C-terminal region with the Citrobacter freundii Eae protein. We have constructed and purified a maltose-binding fusion protein (MBP) containing the product of the entire eae gene of the DEPEC strain 4221. Binding of MBP-Eae(DEPEC) fusion protein to HEp-2 cells was demonstrated by immunofluorescence microscopy. In addition, the Eae protein of DEPEC (4221) demonstrated a strong serological relationship with that of EPEC (E2348/69) as observed using a polyclonal antiserum against MBP-Eae(DEPEC) fusion protein.
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