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Listeria monocytogenes is a foodborne pathogen that poses significant challenges to food safety and public health due to its ability to adapt to harsh environments, particularly those found in food processing facilities. This review explores the global transcriptional responses of L. monocytogenes to various chemical oxidants, including hydrogen peroxide, chlorine dioxide, ozone, and plasma-activated water. By comparing the transcriptomic data of multiple studies, we identified the differentially expressed genes associated with key cellular processes, including oxidative stress responses, cell envelope biosynthesis, metabolic adaptation, efflux mechanisms, and virulence regulation. This review demonstrates that L. monocytogenes employs distinct gene expression patterns to resist disinfectant stress, primarily by upregulating efflux pumps, reactive oxygen species detoxification mechanisms, and DNA repair pathways as well as modulating central metabolism. Several disinfection treatments commonly affect the key genes related to peptidoglycan biosynthesis, cell envelope, cell division, glycolysis, oxidative stress response, and chemotaxis. Although oxidizing agents induce widely conserved gene expression patterns, other treatments trigger unique responses. However, interpretation of different study findings is restricted by methodological inconsistencies, including variations in treatment conditions, media, bacterial states, and transcriptomic techniques. These variations and nonuniform fold change thresholds for differentially expressed genes complicate the comparison of different studies. Therefore, standardized frameworks are necessary to elucidate the adaptive responses of L. monocytogenes and refine its disinfection methods in food processing.
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http://dx.doi.org/10.1111/1541-4337.70260 | DOI Listing |
Crit Rev Microbiol
September 2025
Austrian Competence Centre for Food and Feed Quality, Safety and Innovation, FFoQSI GmbH, Tulln, Austria.
Foodborne illness is a critical food safety and public health concern, often resulting from contamination events by resident pathogens in food processing environments (FPEs). , the causative agent of listeriosis, can persist in FPEs over long time periods. Despite rigorous research on the phenotypic and genotypic traits of , no clear pattern has arisen to explain why some strains are able to persist.
View Article and Find Full Text PDFDrug Des Devel Ther
September 2025
Mardin Artuklu University, Kızıltepe Faculty of Agricultural Sciences and Technologies, Department of Field Crops, Mardin, Artuklu, 47200, Türkiye.
Objective: This study was conducted to determine and compare the antioxidant, cytotoxic, and antimicrobial effects of spindle leaves of L. () (oleaster) leaves.
Methods: Total phenolic content was measured using the Folin-Ciocalteu method, phenolic compound analysis by liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) and antimicrobial effect by the minimum inhibition concentration (MIC) method.
Microbiologyopen
October 2025
Department of Food Science, Stellenbosch University, Stellenbosch, Western Cape, South Africa.
Listeria monocytogenes is pervasive in agricultural environments and difficult to eradicate from food-processing facilities. Consequently, various foods become contaminated, posing health risks to immunocompromised individuals. This surveillance study aimed to enhance the understanding of the genetic diversity, virulence, plasmid content, sanitizer tolerance, and antibiotic resistance of L.
View Article and Find Full Text PDFJ Agric Food Chem
September 2025
School of Life Science, Huaibei Normal University, Huaibei 235000, China.
32 was isolated from traditional Chinese fermented long beans. Plantaricin 32, a novel bacteriocin, was purified from 32 fermentation broth. The molecular weight of plantaricin 32 is 956 Da, and its amino acid sequence is N-Arg-Gly-Pro-Gly-Lys-Thr-Asp-Glu-OH.
View Article and Find Full Text PDFCrit Rev Immunol
September 2025
Department of Pharmacy, Birla Institute of Technology and Science (BITS) Pilani, Hyderabad Campus, Dist. Medchal,500078, Telangana State, India.
Caseinolytic protease P (ClpP) is a highly conserved serine protease that plays a pivotal role in protein homeostasis and quality control in bacteria, mitochondria of mammalian cells, and plant chloroplasts. As the proteolytic core of the ATP-dependent Clp protease complex, ClpP partners with regulatory ATPases (e.g.
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