title: Fold-change detection in a whole-pathway model of Escherichia coli chemotaxis.
abstract: There has been recent interest in sensory systems that are able to display a response which is proportional to a fold change in stimulus concentration, a feature referred to as fold-change detection (FCD). Here, we demonstrate FCD in a recent whole-pathway mathematical model of Escherichia coli chemotaxis. FCD is shown to hold for each protein in the signalling cascade and to be robust to kinetic rate and protein concentration variation. Using a sensitivity analysis, we find that only variations in the number of receptors within a signalling team lead to the model not exhibiting FCD. We also discuss the ability of a cell with multiple receptor types to display FCD and explain how a particular receptor configuration may be used to elucidate the two experimentally determined regimes of FCD behaviour. All findings are discussed in respect of the experimental literature.
authors.affiliation: Department of Mathematics & Statistics, University of Reading, Whiteknights, PO Box 220, Reading, RG6 6AX, UK, m.p.edgington@pgr.reading.ac.uk.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Edgington
authors.forename: Marcus J
authors.initials: MJ
authors.lastname: Tindall
mesh_terms: D001426:Bacterial Proteins / Q000502:physiology; D002633:Chemotaxis / Q000502:physiology*; D003198:Computer Simulation; D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000502:physiology; D007700:Kinetics; D008565:Membrane Proteins / Q000502:physiology; D000072236:Methyl-Accepting Chemotaxis Proteins; D008954:Models, Biological; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; C489103:CheW protein, E coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins