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Microorganisms produce functional amyloids that can be examined and manipulated  in vivo  and  in vitro .  Escherichia coli  assemble extracellular adhesive amyloid fibers termed curli that mediate adhesion and promote biofilm formation. We have characterized the dye binding properties of the hallmark amyloid dye, Congo red, with curliated  E .  coli  and with isolated curli fibers. Congo red binds to curliated whole cells, does not inhibit growth, and can be used to comparatively quantify whole-cell curliation. Using Surface Plasmon Resonance, we measured the binding and dissociation kinetics of Congo red to curli. Furthermore, we determined that the binding of Congo red to curli is pH-dependent and that histidine residues in the CsgA protein do not influence Congo red binding. Our results on  E .  coli  strain MC4100, the most commonly employed strain for studies of  E .  coli  amyloid biogenesis, provide a starting point from which to compare the influence of Congo red binding in other  E .  coli  strains and amyloid-producing organisms.

Congo Red Interactions with Curli-Producing E. coli and Native Curli Amyloid Fibers