Protein expression by Listeria monocytogenes grown on a RTE-meat matrix

2008 ◽  
Vol 128 (2) ◽  
pp. 203-211 ◽  
Author(s):  
Sana Mujahid ◽  
Tibor Pechan ◽  
Chinling Wang
Keyword(s):  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Meat Matrix

Effects of Suspension in Emulsified Wiener or Incubation in Wiener Packages on the Virulence of Listeria monocytogenes Scott A in Intragastrically Inoculated A/J Mice†

2005 ◽  
Vol 68 (3) ◽  
pp. 597-601 ◽  
Author(s):  
NANCY G. FAITH ◽  
MARK L. TAMPLIN ◽  
DARRELL BAYLES ◽  
JOHN B. LUCHANSKY ◽  
CHARLES J. CZUPRYNSKI
Keyword(s):  
Listeria Monocytogenes ◽  
Gastrointestinal Tract ◽  
Meat Products ◽  
Brain Heart Infusion ◽  
Systemic Infection ◽  
Brain Heart Infusion Broth ◽  
Harsh Environment ◽  
Meat Matrix

Several outbreaks of listeriosis have been associated with contamination of wieners and other ready-to-eat meat products. In this study, we addressed the question of whether emulsification in, or growth on, wieners triggers a response in the listerial cells that makes them more virulent or protects them against the harsh environment of the gastrointestinal tract in mice. Our results indicate that Listeria monocytogenes Scott A grows poorly, if at all, in one brand of commercially prepared wieners inoculated with 5 × 103 to 5 × 106 CFU per package and incubated at 15°C. Neither L. monocytogenes Scott A emulsified in a slurry of homogenized wieners nor recovered from wiener package fluid after a 7-day incubation at 15°C were more virulent when inoculated into the stomachs of A/J mice than L. monocytogenes Scott A grown in brain heart infusion broth. These findings suggest that the ability of L. monocytogenes Scott A to cause systemic infection following introduction into the gastrointestinal tract was not improved by incubation with wieners or suspension in a meat matrix.

Proteomic Analysis of a Hypochlorous Acid–Tolerant Listeria monocytogenes Cultural Variant Exhibiting Enhanced Biofilm Production

2007 ◽  
Vol 70 (5) ◽  
pp. 1129-1136 ◽  
Author(s):  
JAMES P. FOLSOM ◽  
JOSEPH F. FRANK
Keyword(s):  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Ribosomal Protein ◽  
Hypochlorous Acid ◽  
Binding Protein ◽  
Acid Tolerance ◽  
Sugar Binding ◽  
Biofilm Production ◽  
Unknown Protein ◽  
Acid Tolerant

Following exposure of Listeria monocytogenes Scott A (SA) to hypochlorous acid, rough colony variants were identified that were tolerant of hypochlorous acid and produced increased amounts of biofilm. A derivative of one of these variants was smooth, produced even more biofilm, and exhibited greater biofilm chlorine resistance. The objective of this research was to compare the protein expression of a cultural variant to SA and to identify proteins that might be associated with biofilm production and chlorine tolerance. Suspension chlorine tolerance for several cultural variants (SAR, SAR5, and SBS) was determined by exposure to 60 to 120 ppm of hypochlorous acid for 5 min. Hypochlorous acid tolerance of biofilms was determined after growing biofilms on stainless steel and then exposing them to 200 ppm of hypochlorous acid for 5 min. All cultural variants were able to survive 120 ppm of hypochlorous acid in suspension. There was little difference in the hypochlorous acid tolerance of the cultural variant planktonic cells. The cultural variants produced greater amounts of biofilm than the common form of L. monocytogenes and were more tolerant of hypochlorous acid. The SBS variant was selected for proteomic comparison because it was the variant that produced the most biofilm and was the most tolerant of hypochlorous acid when grown as a biofilm. Protein expression of planktonic and biofilm cells of SBS was compared to SA by two-dimensional difference gel electrophoresis. The 50s ribosomal protein, L10, was down-regulated in biofilm SBS. Other proteins down-regulated in planktonic SBS were the peroxide resistance protein (Dpr) and a sugar-binding protein (LMO0181). This sugar-binding protein was also up-regulated in biofilm SBS. One protein spot down-regulated in planktonic SBS contained both 50s ribosomal protein L7/L12 and an unknown protein (LMO1888).

A novel Triticum durum Annexin 12 protein: Expression, purification and biological activities against Listeria monocytogenes growth in meat under refrigeration

2020 ◽  
Vol 143 ◽  
pp. 104143
Author(s):  
Anis Ben Hsouna ◽  
Rania Ben Saad ◽  
Imen Trabelsi ◽  
Walid Ben Romdhane ◽  
Faiçal Brini ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Triticum Durum ◽  
Biological Activities

scholarly journals Use of Two-Dimensional Electrophoresis To Study Differential Protein Expression in Divercin V41-Resistant and Wild-Type Strains of Listeria monocytogenes

2000 ◽  
Vol 66 (10) ◽  
pp. 4318-4324 ◽  
Author(s):  
Frederique Duffes ◽  
Paul Jenoe ◽  
Patrick Boyaval
Keyword(s):  
Transcriptional Regulation ◽  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Sensitive Strain ◽  
Cell Protein ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Resistant Variant ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

ABSTRACT The use of bacteriocins from food-grade lactic acid bacteria to fight against the food-borne pathogen Listeria monocytogenes has been gaining interest. However, the emergence of resistant cells is frequently reported when Listeria is exposed to such antibacterials. A two-dimensional electrophoresis study of whole-cell protein expression of Listeria monocytogenes variants sensitive or resistant to the action of a bacteriocin produced by Carnobacterium divergens V41, divercin V41, is reported in this paper. The resistant variant obtained from the sensitive strain of L. monocytogenes P was also resistant to piscicocins V1 and SF668, but remained sensitive to nisin. Its growth rate was 50% less than the sensitive strain, and the MIC for it was 104 times higher. No reversion of the resistance was observed after 20 successive cultures in the absence of divercin V41. Comparison of the protein patterns by two-dimensional gel electrophoresis analysis showed clear differences. In the resistant variant pattern, at least nine spots had disappeared and eight new ones were observed. One of the newly synthesized proteins was identified as a flagellin of L. monocytogenes. Direct interaction between flagellin and divercin V41 was not evidenced. Intracellular synthesis of flagellin is probably an indirect effect of a modification in transcriptional regulation with widespread effects through a sigma factor. An intense protein, only present in the sensitive strain, was identified as a non-heme iron-binding ferritin displaying strong similarities to Dps proteins. Common modifications in the transcriptional regulation for these two proteins are discussed.

scholarly journals Specific role of the tight junction proteins occludin and claudin-5 on the blood–brain barrier during Listeria monocytogenes infection

2020 ◽  
Vol 76 (06) ◽  
pp. 6416-2020
Author(s):  
JINGJING REN ◽  
MINGWEI YANG ◽  
PENGYAN WANG ◽  
JIANJUN JIANG ◽  
GENQIANG YAN
Keyword(s):  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Tight Junction ◽  
Western Blot ◽  
Blood Brain Barrier ◽  
Evans Blue ◽  
Expression Level ◽  
Brain Barrier ◽  
Protein Expression Level ◽  
Listeria Monocytogenes Infection

To investigate the blood-brain barrier (BBB) permeability of mice after Listeria monocytogenes infection for further study on the mechanism of L. monocytogenes crossing the BBB, a mouse model was established and Evans blue assay was performed to assess the BBB disruption. Using relative quantitative real-time PCR, the RNA expression of Zonula occludens-1 (ZO-1), occludin and claudin-5 were detected. In addition, the protein expression level of ZO-1, occludin and claudin-5 were detected by immunohistochemistry and western blot. The extravasation of Evans blue dye was significantly different between 24 h and 96 h (P < 0.05). The mRNA expression of occludin and claudin-5 were down-regulated than that of the control group at each sampling point (P < 0.05) and ZO-1 showed a significant change at 96 h (P < 0.05). In addition, the protein expression level of occludin and claudin-5 decreased significantly at 48 h and 96 h (P < 0.05) by immunohistochemistry and western blot, compared with the control, while ZO-1 was almost unchanged (P > 0.05). All results indicating that the tight junction integrity of endothelial cells was destroyed and BBB permeability was enhanced in the process of L. monocytogenes infection, and this change was related to the decrease of the expression occludin and claudin-5.

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