A bacterial pathogen that is important in both urinary tract and intestinal infections is Escherichia coli which expresses Dr or related adhesins. In this report, we present a model for testing cell-cell interaction, using both molecularly characterized laboratory cells that express recombinant molecules of human decay-accelerating factor (DAF), and recombinant bacterial Dr colonization factors. Dr adhesin ligand was identified as DAF (CD55), a membrane protein that protects autologous tissues from damage due to the complement system. Structure-function studies mapped the adhesin-binding site on the DAF molecule. A single-point substitution in the third short consensus repeat domain, Ser165 to Leu, corresponding to the Dra to Drb allelic polymorphism, caused complete abolition of adhesin binding to DAF.
Short consensus repeat-3 domain of recombinant decay-accelerating factor is recognized by Escherichia coli recombinant Dr adhesin in a model of a cell-cell interaction.
B Nowicki, A Hart, K E Coyne, D M Lublin, S Nowicki; Short consensus repeat-3 domain of recombinant decay-accelerating factor is recognized by Escherichia coli recombinant Dr adhesin in a model of a cell-cell interaction.. J Exp Med 1 December 1993; 178 (6): 2115–2121. doi: https://doi.org/10.1084/jem.178.6.2115
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