A proteomic approach to study the acid response in Listeria monocytogenes.

Abstract

The responses of Listeria monocytogenes to acidic conditions were studied at the level of protein synthesis at a lethal acidic pH (acid stress) and an intermediary nonlethal acidic pH (acid adaptation). The radiolabeled acid-induced proteins were separated by two-dimensional (2-D) electrophoresis and analyzed by a computer-aided 2-D gel analysis system. The two acidic conditions upgraded a number of constitutive proteins and induced synthesis of a number of novel proteins. The majority of these induced proteins were common to the two pHs and the lethal acidic pH induced more proteins than the mildly acidic pH, suggesting that the responses to the two acidic conditions involve many common proteins and that additional proteins are required when the bacteria have to face more severe acidic conditions. In waiting for identification of more proteins involved in order to have a wholesome mechanistic picture of the acid response in L. monocytogenes, we present here the first results obtained from identification of the most abundant of these acid-induced proteins using peptide mass fingerprinting and matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) technique.