Proteins of the food-borne pathogen <i>Listeria monocytogenes</i> strain F2365 relevant to lethal acidic stress and during rapid inactivation

Abstract

<abstract> <p><italic>Listeria monocytogenes</italic>, which causes human listeriosis after consumption of contaminated food, can adapt and survive under a wide range of physiological and chemical stresses. In this study, the overall proteomic response of the <italic>L. monocytogenes</italic> strain F2365—a strain with mutations limiting its ability to tolerate acidic conditions—to progressive non-thermal acidic inactivation was investigated. The challenge process was investigated in the early stationary growth phase where F2365 cultures were acidified (pH 3.0, HCl) at 5 min, 1 h, and 2 h, generating pH 4.8, pH 4.1, and pH 3.5, respectively, with protein abundance measured using iTRAQ. Approximately 73 proteins increased in abundance and 8 declined when acidic stress became non-growth-permissive (pH < 4.1) and inactivation accelerated to approximately 2 log units/h. The functional categories of responding proteins were broad but the proteins involved were specific in nature and did not include whole pathways. Many responses likely accentuate energy conservation and compensate vital metabolic processes. For example, further repression of FlaA, normally repressed under acidic stress, occurs accompanied by an increase in quinol oxidase subunit QoxA and glycerol kinase GlpK. Proteins maintaining cell wall integrity, such as Iap and CwlO, manifested the overall largest abundance increase trend. Virulence proteins were also induced, including InlA, InlC, Hyl, Mpl, PlcA, and PlcB, suggesting that acidification may have mimicked conditions inducing some host survival traits. The overall suite of proteins affected appears to be the "last ditch" responses to non-thermal inactivation above and beyond the standard protections afforded in the stationary-growth phase. The array of proteins found here may provide a deeper understanding of the physiological responses of this pathogen during non-thermal inactivation.</p> </abstract>