4.7 Article

Proteomic analysis reveals differential responses of Listeria monocytogenes to free and nanoencapsulated nisin

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ELSEVIER
DOI: 10.1016/j.ijfoodmicro.2021.109170

关键词

Listeria; Nisin; Stress response; Liposomes; Nanovesicles; Proteomics

资金

  1. CNPq (Brasilia, Brazil) [306936/20178]
  2. CAPES

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This study investigated how L. monocytogenes responded to sublethal doses of nisin and nisin-loaded liposomes by examining its proteome regulation, identifying changes in protein expression levels related to various cellular functions. The results showed alterations in protein expression associated with ABC transporter systems, transmembrane proteins, RNA-binding proteins, and stress response proteins, indicating the specific response of L. monocytogenes to nisin treatments. Moreover, the encapsulation of nisin in liposomes led to reduced stress response factors expression and potential implications for nisin resistance development.
The ability of Listeria monocytogenes grow on ready-to-eat food is a major concern in food safety. Natural antimicrobials, such as nisin, can be used to control this pathogen, but the increasing reports of nisin tolerance and resistance make necessary novel approaches to increase its effectiveness, such as encapsulation. The goal of this study was to investigate how L. monocytogenes ATCC7644 regulates and shapes its proteome in response to sublethal doses of nisin and nisin-loaded phosphatidylcholine liposomes (lipo-nisin), compared to untreated cells growing under optimal conditions. Total proteins were extracted from L. monocytogenes cells treated for 1 h with free and lipo-nisin. As result, of 803 proteins that were initially identified, 64 and 53 proteins were differentially upregulated and downregulated respectively, in the treatments with nisin and lipo-nisin. Changes of Listeria proteome in response to treatments containing nisin were mainly related to ATP-binding cassette (ABC) transporter systems, transmembrane proteins, RNA-binding proteins and diverse stress response proteins. Some of the proteins uniquely detected in samples treated with free nisin were the membrane proteins SecD, Lmo1539 and the YfhO enzyme, which are related to translocation of L. monocytogenes virulence factors, activation of the LiaRmediated stress defense and glycosylation of wall teichoic acid, respectively. The L. monocytogenes treated with liposome encapsulated nisin showed no expression of some stress response factors as compared with the free nisin, suggesting a reduction of stress mediated response and production of nisin-resistance factors by exposure to encapsulated nisin.

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