Feb 13, 2001

The role of pyridoxal phosphate in the function of EspB, a protein secreted by enteropathogenic Escherichia coli

FEBS Letters
K A TaylorM S Donnenberg


The sequence of EspB, a secreted protein required for virulence of enteropathogenic Escherichia coli (EPEC), reveals a motif common to enzymes that bind pyridoxal phosphate. Pyridoxal phosphate was not found by fluorometry in concentrated supernatants of EPEC cultures that contain EspB. Plasmids containing cloned espB, in which the lysine residue conserved in the motif was substituted with either an arginine or methionine residue, remained capable of complementing an espB deletion mutant to restore EspB function. The results of these studies do not support a role for pyridoxal phosphate in EspB function.

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Mentioned in this Paper

Alkalescens-Dispar Group
Enzymes, antithrombotic
Gene Deletion Abnormality
Outer Membrane Lipoproteins, Bacterial
Pyridoxal Phosphate
Staphylococcal Protein A

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