Immunoproteome profiling of Listeria monocytogenes under mild acid and salt stress conditions

Listeria monocytogenes is one of the main foodborne pathogens worldwide. Although its response to stress conditions has been extensively studied, it is still present in the food processing environments and is a concern for consumers. To investigate how this microorganism adapts its proteome in mild stress conditions, a combined proteomics and bioinformatics approach was used to characterize the immunogenic protein profile of a sequence type 7 (ST7) strain that caused severe listeriosis outbreaks in central Italy. Extracted proteins were analyzed by immunoblotting using positive sera against L. monocytogenes and nLC-ESI-MS/MS, and all data were examined by five software to predict subcellular localization (SCL). A total of 226 proteins were extracted from the bands of interest, 58 of which were classified as potential immunogenic antigens. Compared to control cells grown under optimal conditions, six proteins, some of which under-described, were expressed under mild acid and salt stress conditions and/or at 12 degrees C. In particular, adaptation and shaping of the proteome mainly involved cell motility at 12 degrees C without acid and salt stress, whereas the combination of the same temperature with mild acid and salt stress induced a response concerning carbohydrate metabolism, oxidative stress, and DNA repair. Raw data are available via ProteomeXchange with identifier PXD033519.

Automated summary

This study characterized the immunogenic protein profile of a sequence type 7 (ST7) strain of Listeria monocytogenes that caused severe listeriosis outbreaks in central Italy using a combined proteomics and bioinformatics approach. The results showed that the proteome of L. monocytogenes adapted and reshaped under mild stress conditions, involving cell motility, carbohydrate metabolism, oxidative stress, and DNA repair.