An overview of stress response proteomes in Listeria monocytogenes

Abstract

Listeria monocytogenes adapts to diverse stress conditions including cold, osmotic, heat, acid, and alkali stresses encountered during food processing and preservation which is a serious food safety threat. In this review, we have presented the major findings on this bacterium’s stress response proteomes to date along with the different approaches used for its proteomic analysis. The key proteome findings on cold, heat shock, salt, acid, alkaline and HHP stresses illustrate that the cellular stress responses in this organism are a culmination of multiple protein expression changes in response to a particular stress stimuli. Moreover, a number of key proteins may be involved in conferring the cross protective effects against various stress environments. As an example, ferritin-like protein (designated as Fri or Flp) is induced during cold, heat, and HHP stresses. Similarly, general stress protein Ctc is induced in cold and osmotic stresses while molecular chaperones such as GroEL and DnaK are induced in cold and heat stresses. Furthermore, a number of stress proteins also contribute towards L. monocytogenes virulence and pathogenicity. Future research may lead to understanding the stress proteomes of this pathogen induced on various food matrices and processing environments in which it can persist for long periods of time.