The role of bacterial microcompartments in Listeria monocytogenes growth, stress adaptation and virulence

2021 ◽  
Author(s):  
Zhe Zeng
Keyword(s):  
Listeria Monocytogenes ◽  
Growth Stress ◽  
Stress Adaptation ◽  
Bacterial Microcompartments

scholarly journals Bacterial microcompartments linked to the flavin-based extracellular electron transfer drives anaerobic ethanolamine utilization in Listeria monocytogenes

2020 ◽  
Author(s):  
Zhe Zeng ◽  
Sjef Boeren ◽  
Varaang Bhandula ◽  
Samuel H. Light ◽  
Eddy J. Smid ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Listeria Monocytogenes ◽  
Electron Acceptor ◽  
Cell Membranes ◽  
Anaerobic Growth ◽  
Extracellular Electron Transfer ◽  
Severe Illness ◽  
Redox Imbalance ◽  
Bacterial Microcompartments

AbstractEthanolamine (EA) is a valuable microbial carbon and nitrogen source derived from phospholipids present in cell membranes. EA catabolism is suggested to occur in so-called bacterial microcompartments (BMCs) and activation of EA utilization (eut) genes is linked to bacterial pathogenesis. Despite reports showing that activation of eut in Listeria monocytogenes is regulated by a vitamin B12-binding riboswitch and that upregulation of eut genes occurs in mice, it remains unknown whether EA catabolism is BMC dependent. Here, we provide evidence for BMC-dependent anaerobic EA utilization via metabolic analysis, proteomics and electron microscopy. First, we show B12-induced activation of the eut operon in L. monocytogenes coupled to uptake and utilization of EA thereby enabling growth. Next, we demonstrate BMC formation in conjunction to EA catabolism with the production of acetate and ethanol in a molar ratio of 2:1. Flux via the ATP generating acetate branch causes an apparent redox imbalance due to reduced regeneration of NAD+ in the ethanol branch resulting in a surplus of NADH. We hypothesize that the redox imbalance is compensated by linking eut BMC to anaerobic flavin-based extracellular electron transfer (EET). Using L. monocytogenes wild type, a BMC mutant and a EET mutant, we demonstrate an interaction between BMC and EET and provide evidence for a role of Fe3+ as an electron acceptor. Taken together, our results suggest an important role of anaerobic BMC-dependent EA catabolism in the physiology of L. monocytogenes, with a crucial role for the flavin-based EET system in redox balancing.IMPORTANCEListeria monocytogenes is a food-borne pathogen causing severe illness and, as such, it is crucial to understand the molecular mechanisms contributing to pathogenicity. One carbon source that allows L. monocytogenes to grow in humans is ethanolamine (EA), which is derived from phospholipids present in eukaryotic cell membranes. It is hypothesized that EA utilization occurs in bacterial microcompartments (BMCs), self-assembling subcellular proteinaceous structures and analogs of eukaryotic organelles. Here, we demonstrate that BMC-driven utilization of EA in L. monocytogenes results in increased energy production essential for anaerobic growth. However, exploiting BMCs and the encapsulated metabolic pathways also requires balancing of oxidative and reductive pathways. We now provide evidence that L. monocytogenes copes with this by linking BMC activity to flavin-based extracellular electron transfer (EET) using iron as an electron acceptor. Our results shed new light on an important molecular mechanism that enables L. monocytogenes to grow using host-derived phospholipid degradation products.

scholarly journals Bacterial Microcompartments Coupled with Extracellular Electron Transfer Drive the Anaerobic Utilization of Ethanolamine in Listeria monocytogenes

mSystems ◽  
2021 ◽  
Vol 6 (2) ◽  
Author(s):  
Zhe Zeng ◽  
Sjef Boeren ◽  
Varaang Bhandula ◽  
Samuel H. Light ◽  
Eddy J. Smid ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Listeria Monocytogenes ◽  
Electron Acceptor ◽  
Cell Membranes ◽  
Extracellular Electron Transfer ◽  
Vitamin B ◽  
Content Type ◽  
Redox Imbalance ◽  
Bacterial Microcompartments

ABSTRACT Ethanolamine (EA) is a valuable microbial carbon and nitrogen source derived from cell membranes. EA catabolism is suggested to occur in a cellular metabolic subsystem called a bacterial microcompartment (BMC), and the activation of EA utilization (eut) genes is linked to bacterial pathogenesis. Despite reports showing that the activation of eut is regulated by a vitamin B12-binding riboswitch and that upregulation of eut genes occurs in mice, it remains unknown whether EA catabolism is BMC dependent in Listeria monocytogenes. Here, we provide evidence for BMC-dependent anaerobic EA utilization via metabolic analysis, proteomics, and electron microscopy. First, we show vitamin B12-induced activation of the eut operon in L. monocytogenes coupled to the utilization of EA, thereby enabling growth. Next, we demonstrate BMC formation connected with EA catabolism with the production of acetate and ethanol in a molar ratio of 2:1. Flux via the ATP-generating acetate branch causes an apparent redox imbalance due to the reduced regeneration of NAD+ in the ethanol branch resulting in a surplus of NADH. We hypothesize that the redox imbalance is compensated by linking eut BMCs to anaerobic flavin-based extracellular electron transfer (EET). Using L. monocytogenes wild-type, BMC mutant, and EET mutant strains, we demonstrate an interaction between BMCs and EET and provide evidence for a role of Fe3+ as an electron acceptor. Taken together, our results suggest an important role of BMC-dependent EA catabolism in L. monocytogenes growth in anaerobic environments like the human gastrointestinal tract, with a crucial role for the flavin-based EET system in redox balancing. IMPORTANCE Listeria monocytogenes is a foodborne pathogen causing severe illness, and as such, it is crucial to understand the molecular mechanisms contributing to pathogenicity. One carbon source that allows L. monocytogenes to grow in humans is ethanolamine (EA), which is derived from phospholipids present in eukaryotic cell membranes. It is hypothesized that EA utilization occurs in bacterial microcompartments (BMCs), self-assembling subcellular proteinaceous structures and analogs of eukaryotic organelles. Here, we demonstrate that BMC-driven utilization of EA in L. monocytogenes results in increased energy production essential for anaerobic growth. However, exploiting BMCs and the encapsulated metabolic pathways also requires the balancing of oxidative and reductive pathways. We now provide evidence that L. monocytogenes copes with this by linking BMC activity to flavin-based extracellular electron transfer (EET) using iron as an electron acceptor. Our results shed new light on an important molecular mechanism that enables L. monocytogenes to grow using host-derived phospholipid degradation products.

The role of PhoP/PhoQ two component system in regulating stress adaptation in Cronobacter sakazakii

2021 ◽  
pp. 103851
Author(s):  
Yan Ma ◽  
Yingying Zhang ◽  
Ke Chen ◽  
Lingzhu Zhang ◽  
Yibei Zhang ◽  
...  
Keyword(s):  
Stress Adaptation ◽  
Cronobacter Sakazakii ◽  
Two Component System ◽  
Component System ◽  
Two Component

scholarly journals The Phosphoarginine Phosphatase PtpB from Staphylococcus aureus Is Involved in Bacterial Stress Adaptation during Infection

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 645
Author(s):  
Mohamed Ibrahem Elhawy ◽  
Sylvaine Huc-Brandt ◽  
Linda Pätzold ◽  
Laila Gannoun-Zaki ◽  
Ahmed Mohamed Mostafa Abdrabou ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Staphylococcus Aureus ◽  
Treatment Strategies ◽  
Physiological Role ◽  
Aureus Strain ◽  
Stress Adaptation ◽  
Cellular Mechanisms ◽  
Host Interaction ◽  
Liver And Kidney

Staphylococcus aureus continues to be a public health threat, especially in hospital settings. Studies aimed at deciphering the molecular and cellular mechanisms that underlie pathogenesis, host adaptation, and virulence are required to develop effective treatment strategies. Numerous host-pathogen interactions were found to be dependent on phosphatases-mediated regulation. This study focused on the analysis of the role of the low-molecular weight phosphatase PtpB, in particular, during infection. Deletion of ptpB in S. aureus strain SA564 significantly reduced the capacity of the mutant to withstand intracellular killing by THP-1 macrophages. When injected into normoglycemic C57BL/6 mice, the SA564 ΔptpB mutant displayed markedly reduced bacterial loads in liver and kidney tissues in a murine S. aureus abscess model when compared to the wild type. We also observed that PtpB phosphatase-activity was sensitive to oxidative stress. Our quantitative transcript analyses revealed that PtpB affects the transcription of various genes involved in oxidative stress adaptation and infectivity. Thus, this study disclosed first insights into the physiological role of PtpB during host interaction allowing us to link phosphatase-dependent regulation to oxidative bacterial stress adaptation during infection.

scholarly journals Role of Branched-Chain Fatty Acids in pH Stress Tolerance in Listeria monocytogenes

2006 ◽  
Vol 73 (3) ◽  
pp. 997-1001 ◽  
Author(s):  
Efstathios S. Giotis ◽  
David A. McDowell ◽  
Ian S. Blair ◽  
Brian J. Wilkinson
Keyword(s):  
Fatty Acids ◽  
Listeria Monocytogenes ◽  
Stress Tolerance ◽  
Ph Sensitive ◽  
Branched Chain Fatty Acids ◽  
Alkaline Conditions ◽  
Branched Chain ◽  
Ph Adaptation ◽  
Chain Fatty Acids

ABSTRACT In alkaline conditions, Listeria monocytogenes cells develop higher proportions of branched-chain fatty acids (FAs), including more anteiso forms. In acid conditions, the opposite occurs. Reduced growth of pH-sensitive mutants at adverse pH (5.0/9.0) was alleviated by the addition of 2-methylbutyrate (an anteiso-FA precursor), suggesting that anteiso-FAs are important in adaptation to adverse pH. The balance between anteiso- and iso-FAs may be more important than changes in the amounts and/or degrees of saturation of FAs in pH adaptation.

scholarly journals Listeria monocytogenes: An emerging food-borne pathogen and its public health implications

2016 ◽  
Vol 10 (02) ◽  
pp. 149-154 ◽  
Author(s):  
Waffa W Reda ◽  
Khaled Abdel-Moein ◽  
Ahmed Hegazi ◽  
Yasmin Mohamed ◽  
Khaled Abdel-Razik
Keyword(s):  
Listeria Monocytogenes ◽  
Raw Milk ◽  
Food Samples ◽  
Food Borne ◽  
Contaminated Food ◽  
Luncheon Meat ◽  
Stool Specimens ◽  
Polymerase Chain ◽  
Minced Meat

Introduction: Listeria monocytogenes is considered one of the most important food-borne pathogens transmitted to humans via contaminated food. The aim of the present study was to demonstrate the importance of L. monocytogenes as a food-borne pathogen. Methodology: A total of 340 samples were collected from different localities in El Giza Governorate, Egypt, to check the occurrence of L. monocytogenes in that area. The collected samples comprised 250 food samples, 40 swabs from food refrigerators, and 50 stool specimens from diarrheic children. L. monocytogenes was isolated from the examined samples according to the International Organization for Standardization. The isolates were tested biochemically using Listeria Microbact 12L and confirmed by polymerase chain reaction. Results: The isolation rates of L. monocytogenes were 8% in beef burger, 4% in minced meat, 4% in luncheon meat, while sausage samples were all negative. Eight percent of raw milk samples were positive for L. monocytogenes, whereas cheese samples and refrigerator swabs were negative. Only Listeria grayi was isolated from human stools (2.5%). Conclusion: The high isolation rates of L. monocytogenes among the examined food stuffs highlight the crucial role of food as an important vehicle for this pathogen. More efforts should be made to ensure safe handling and processing of these foods to reduce the transmission of L. monocytogenes to humans.

scholarly journals The inlA Gene of Listeria monocytogenesLO28 Harbors a Nonsense Mutation Resulting in Release of Internalin

1998 ◽  
Vol 66 (7) ◽  
pp. 3420-3422 ◽  
Author(s):  
Renaud Jonquières ◽  
Hélène Bierne ◽  
Jérôme Mengaud ◽  
Pascale Cossart
Keyword(s):  
Cell Adhesion ◽  
Listeria Monocytogenes ◽  
Virulence Factor ◽  
Adhesion Molecule ◽  
Nonsense Mutation ◽  
Cell Adhesion Molecule ◽  
Culture Medium ◽  
Surface Protein ◽  
Truncated Protein

ABSTRACT Internalin is a surface protein that mediates entry ofListeria monocytogenes EGD into epithelial cells expressing the cell adhesion molecule human E-cadherin or its chicken homolog, L-CAM, which act as receptors for internalin. After observing that entry of L. monocytogenes LO28 into S180 fibroblasts, in contrast to that of EGD, did not increase after transfection with L-CAM, we examined both the expression and the structure of internalin in strain LO28. We discovered a nonsense mutation in inlA which results in a truncated protein released in the culture medium. Mutations leading to release of internalin were also detected in clinical and food isolates. These results question the role of internalin as a virulence factor in murine listeriosis.

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