Abstract
Listeria monocytogenes is an organism associated with a wide range of foods. It causes listeriosis, a severe illness that mainly affects people with weakened immune systems. Proteomic profiles of three different L. monocytogenes isolates were studied using 1D SDS PAGE, 2DE and mass spectrometry. The protein banding patterns generated by 1D SDS PAGE of three strains of L. monocytogenes were found to be similar. Visual observations from 2DE gel maps revealed that certain spots appeared to have intensity differences. Key differences in proteins synthesis of three strains of L. monocytogenes were found using the PDQest TM 2DE Analysis software. Comparison showed that the clinical isolate (strain SB92/844) had 53.4% and 53.9% protein profile similarity with dairy isolate (strain V7) and seafood isolate (SB92/870), respectively. The identity of selected protein spots was achieved using MALDI-TOF and ion trap mass spectrometry. It was found that certain identified proteins (i.e., a major cold shock protein and superoxide dismutase) were expressed differently between two local strains of L. monocytogenes (SB92/844, SB92/870) and one strain from overseas (V7).
Highlights
IntroductionThe genus, Listeria, is classified in the family Listeriaceae (previously known as Corynebacteriaceae) with microbiological features, such as non-spore forming, catalase-positive and oxidase-negative
The genus, Listeria, is classified in the family Listeriaceae with microbiological features, such as non-spore forming, catalase-positive and oxidase-negative
This study presents an initial view of the protein expression in two strains of L. monocytogenes species in New Zealand
Summary
The genus, Listeria, is classified in the family Listeriaceae (previously known as Corynebacteriaceae) with microbiological features, such as non-spore forming, catalase-positive and oxidase-negative. Two-dimensional (2DE) polyacrylamide gel electrophoresis is the most commonly used technique to study protein changes in L. monocytogenes in response to stresses, such as resistance to antimicrobial chemicals, low pH, high salinity or cold shock. With the development of quantitative proteomics, high-throughput gel- and non-gel-based protein fractionation techniques coupled with protein identification by high-throughput tandem mass spectrometry (MS/MS)-based automated software algorithms are widely used to analyze protein expression in L. monocytogenes. The development of intracellular and extracellular proteome maps of L. monocytogenes has been attempted using multiplexing fluorescent two-dimensional fluorescence difference gel electrophoresis (2D-DIGE) and MALDI-TOF [16,17]. There are limited numbers of proteomics studies that attempt to explore the unique protein machinery of L. monocytogenes strains isolated from different ecological niches [21]. Current research on the proteomics of L. monocytogenes provides a promising future to develop detection technologies based on specific protein markers
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