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Chemoreceptors McpB and McpC in Salmonella enterica have been reported topromote chemotaxis in LB motility-plate assays. Of the chemicals tested aspotential effectors of these receptors, the only response was towardsL-cysteine and its oxidized form, L-cystine. Although enhanced radial migrationin plates suggested positive chemotaxis to both amino acids, capillary assaysfailed to show an attractant response to either, in cells expressing only thesetwo chemoreceptors. In vivo fluorescence resonance energy transfer (FRET)measurements of kinase activity revealed that in wild-type bacteria, cysteineand cystine are chemoeffectors of opposing sign, the reduced form being achemoattractant and the oxidized form a repellent. The attractant response tocysteine was mediated primarily by Tsr, as reported earlier for E. coli. Therepellent response to cystine was mediated by McpB / C. Adaptive recovery uponcystine exposure required the methyl-transferase/-esterase pair, CheR / CheB,but restoration of kinase activity was never complete (i.e. imperfectadaptation). We provide a plausible explanation for the attractant-likeresponses to both cystine and cysteine motility plates, and speculate that theopposing signs of response to this redox pair might afford Salmonella amechanism to gauge and avoid oxidative environments.

Salmonella chemoreceptors McpB and McpC mediate a repellent response to L-cystine: a potential mechanism to avoid oxidative conditions