Proteomics analysis of Listeria monocytogenes ATCC 19115 in response to simultaneous triple stresses

He, Lei; Deng, Qinglin; Chen, Mou-tong; Wu, Qingping; Lü, Yongjun

doi:10.1007/s00203-015-1116-1

Cited by 9 publications

(7 citation statements)

References 34 publications

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“…As for many other bacterial pathogens, L. monocytogenes activates the expression of virulence genes at host body temperature (23). Throughout the years, multiple studies have been published exploring Listeria 's temperature adaptation, either through physicochemical tests (21, 24–29), genomic and transcriptomic methods (30–38), and also through metabolic and proteomic approaches (39–44). However, there is still a knowledge gap in the comparison of subproteomic changes to different temperatures, particularly in the biofilm mode of growth.…”

Section: Introductionmentioning

confidence: 99%

Listeria monocytogenes Biofilm Adaptation to Different Temperatures Seen Through Shotgun Proteomics

Santos

Viala²,

Chambon³

et al. 2019

Front. Nutr.

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Listeria monocytogenes is a foodborne pathogen that can cause invasive severe human illness (listeriosis) in susceptible patients. Most human listeriosis cases appear to be caused by consumption of refrigerated ready-to-eat foods. Although initial contamination levels in foods are usually low, the ability of these bacteria to survive and multiply at low temperatures allows it to reach levels high enough to cause disease. This study explores the set of proteins that might have an association with L. monocytogenes adaptation to different temperatures. Cultures were grown in biofilm, the most widespread mode of growth in natural and industrial realms. Protein extractions were performed from three different growth temperatures (10, 25, and 37°C) and two growth phases (early stage and mature biofilm). L. monocytogenes subproteomes were targeted using three extraction methods: trypsin-enzymatic shaving, biotin-labeling and cell fractionation. The different subproteomes obtained were separated and analyzed by shotgun proteomics using high-performance liquid chromatography combined with tandem mass spectrometry (LC-OrbiTrap LTQVelos, ThermoFisher Scientific). A total of 141 (biotinylation), 98 (shaving) and 910 (fractionation) proteins were identified. Throughout the 920 unique proteins identified, many are connected to basic cell functions, but some are linked with thermoregulation. We observed some noteworthy protein abundance shifts associated with the major adaptation to cold mechanisms present in L. monocytogenes , namely: the role of ribosomes and the stressosome with a higher abundance of the general stress protein Ctc (Rl25) and the general stress transcription factor sigma B (σ B ), changes in cell fluidity and motility seen by higher levels of foldase protein PrsA2 and flagellin (FlaA), the uptake of osmolytes with a higher abundance of glycine betaine (GbuB) and carnitine transporters (OpucA), and the relevance of the overexpression of chaperone proteins such as cold shock proteins (CspLA and Dps). As for 37°C, we observed a significantly higher percentage of proteins associated with transcriptional or translational activity present in higher abundance upon comparison with the colder settings. These contrasts of protein expression throughout several conditions will enrich databases and help to model the regulatory circuitry that drives adaptation of L. monocytogenes to environments.

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Section: Introductionmentioning

confidence: 99%

Listeria monocytogenes Biofilm Adaptation to Different Temperatures Seen Through Shotgun Proteomics

Santos

Viala²,

Chambon³

et al. 2019

Front. Nutr.

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“…Previous studies have carried out proteomics analyses of L. monocytogenes exposed to single-or dual-stress (acid and salt) conditions [5,7,14,[29][30][31][32][33][34][35][36]. However, the response of the proteome of L. monocytogenes to simultaneous exposure to acid and salt for a time-course study had not been investigated and was therefore examined in the present study.…”

Section: Resultsmentioning

confidence: 99%

Impact of Combined Acidic and Hyperosmotic Shock Conditions on the Proteome ofListeria monocytogenesATCC 19115 in a Time-Course Study

Zhang

Bai

Bowman

2019

Journal of Food Quality

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Listeria monocytogenes can cause listeriosis in humans through consumption of contaminated food and can adapt to and grow under a wide array of physiochemical stresses. Consequently, it causes persistent food safety issues and requires vigilant sanitation processes to be in place, especially for the manufacture of high-risk food products. In this study, the global proteomic responses of the food-borne pathogen L. monocytogenes strain ATCC 19115 were determined when exposed to nonthermal inactivation. This process was examined in the early stationary growth phase with the strain placed under simultaneous exposure to low pH (pH 3.5) and high salinity (aw 0.900, 14% NaCl). Proteomic responses, measured using iTRAQ techniques, were conducted over a time course (5 min, 30 min, and 1 h at 25°C). The enumeration results showed that, at 5 min, cells underwent initial rapid inactivation by 1.2 log units and 2.5 log units after 30 min, and after that, culturability remained stable when sampled at 1 h. From the iTRAQ results, the proteome level changes that occur rapidly during the inactivation process mainly affected prophage, cell defense/detoxification, carbohydrate-related metabolism, transporter proteins, phosphotransferase systems, cell wall biogenesis, and specific cell surface proteins. Pathway map analysis revealed that several pathways are affected including pentose and glucuronate interconversions, glycolysis/gluconeogenesis, pyruvate metabolism, valine, leucine and isoleucine biosynthesis, oxidative phosphorylation, and proteins associated with bacterial invasion of epithelial cells and host survival. Proteome profiling provided a better understanding of the physiological responses of this pathogen to adapt to lethal nonthermal environments and indicates the need to improve food processing and storage methods, especially for non- or minimally thermally processed foods.

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“…Overall, adaptation to different antimicrobials leads to modification of the amount of some ribosomal proteins involved in translation, ribosomal structure and biogenesis (30S ribosomal proteins S1, S2, S3, and S8 and 50S ribosomal proteins L5, L7/L12, L25, and L31). Previously, L. monocytogenes cells were shown to decrease the level of S1 protein under combined stresses (low pH, high salinity and low temperature) (He et al, 2015). Guevara et al (2015) showed that the level of L7/L12 increased during moderate heat, carvacrol and thymol treatments.…”

Section: Discussionmentioning

confidence: 99%

“…Despite recent progress in elucidating the details of the L. monocytogenes genome, the mechanisms this bacterium adapts to natural antimicrobial compounds remains largely unclear (NicAogáin and O’Byrne, 2016; Braschi et al, 2018a,b). Studies on the adaptation of L. monocytogenes to natural antimicrobial compounds are crucial to highlight the relationship between stress and virulence and to optimize the protocols used for food production (Chaturongakul et al, 2008; Bowman et al, 2010; He et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

How Listeria monocytogenes Shapes Its Proteome in Response to Natural Antimicrobial Compounds

et al. 2019

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The goal of this study was to investigate the adaptation of L. monocytogenes Scott A cells to treatments with sublethal doses of antimicrobials (ethanol, citral, carvacrol, E-2-hexenal and thyme essential oil). The survival of L. monocytogenes cells was not affected by the antimicrobials at the concentrations assayed, with the exception of ethanol (1% v/v) and thyme essential oil (100 mg/L), which decreased cell viability from 8.53 ± 0.36 to 7.20 ± 0.22 log CFU/mL (P = 0.04). We subsequently evaluated how L. monocytogenes regulates and shapes its proteome in response to antimicrobial compounds. Compared to the control cells grown under optimal conditions, L. monocytogenes treated for 1 h with the antimicrobial compounds showed increased or decreased (≥ or ≤2-fold, respectively, P < 0.05) levels of protein synthesis for 223 protein spots. As shown multivariate clustering analysis, the proteome profiles differed between treatments. Adaptation and shaping of proteomes mainly concerned cell cycle control, cell division, chromosome, motility and regulatory related proteins, carbohydrate, pyruvate, nucleotide and nitrogen metabolism, cofactors and vitamins and stress response with contrasting responses for different stresses. Ethanol, citral (85 mg/l) or (E)-2-hexenal (150 mg/L) adapted cells increased survival during acid stress imposed under model (BHI) and food-like systems.

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Proteomics analysis of Listeria monocytogenes ATCC 19115 in response to simultaneous triple stresses

Cited by 9 publications

References 34 publications

Listeria monocytogenes Biofilm Adaptation to Different Temperatures Seen Through Shotgun Proteomics

Listeria monocytogenes Biofilm Adaptation to Different Temperatures Seen Through Shotgun Proteomics

Impact of Combined Acidic and Hyperosmotic Shock Conditions on the Proteome ofListeria monocytogenesATCC 19115 in a Time-Course Study

How Listeria monocytogenes Shapes Its Proteome in Response to Natural Antimicrobial Compounds

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