scholarly journals The nucleoid-associated proteins H-NS and FIS modulate the DNA supercoiling response of the pel genes, the major virulence factors in the plant pathogen bacterium Dickeya dadantii

2012 ◽  
Vol 40 (10) ◽  
pp. 4306-4319 ◽  
Author(s):  
Zghidi-Abouzid Ouafa ◽  
Sylvie Reverchon ◽  
Thomas Lautier ◽  
Georgi Muskhelishvili ◽  
William Nasser
Keyword(s):  
Virulence Factors ◽  
Plant Pathogen ◽  
Dna Supercoiling ◽  
Dickeya Dadantii ◽  
Associated Proteins

Regulation of pel genes, major virulence factors in the plant pathogen bacterium Dickeya dadantii , is mediated by cooperative binding of the nucleoid-associated protein H-NS

2016 ◽  
Vol 167 (4) ◽  
pp. 247-253 ◽  
Author(s):  
Ouafa Zghidi-Abouzid ◽  
Elodie Hérault ◽  
Sylvie Rimsky ◽  
Sylvie Reverchon ◽  
William Nasser ◽  
...  
Keyword(s):  
Virulence Factors ◽  
Plant Pathogen ◽  
Cooperative Binding ◽  
Dickeya Dadantii

scholarly journals Same tune, different song — cytokinins as virulence factors in plant–pathogen interactions?

2018 ◽  
Vol 44 ◽  
pp. 82-87 ◽  
Author(s):  
Thomas Spallek ◽  
Pamela Gan ◽  
Yasuhiro Kadota ◽  
Ken Shirasu
Keyword(s):  
Virulence Factors ◽  
Plant Pathogen ◽  
Plant Pathogen Interactions

scholarly journals Exploring Virulence Factors and Alternative Therapies against Staphylococcus aureus Pneumonia

Toxins ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 721
Author(s):  
Jelle Vlaeminck ◽  
Dina Raafat ◽  
Kristin Surmann ◽  
Leen Timbermont ◽  
Nicole Normann ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Virulence Factors ◽  
Financial Burden ◽  
Opportunistic Pathogen ◽  
Vaccine Research ◽  
Potential Significance ◽  
Associated Proteins ◽  
Alternative Approaches ◽  
Staphylococcus Aureus Pneumonia ◽  
High Level

Pneumonia is an acute pulmonary infection associated with high mortality and an immense financial burden on healthcare systems. Staphylococcus aureus is an opportunistic pathogen capable of inducing S. aureus pneumonia (SAP), with some lineages also showing multidrug resistance. Given the high level of antibiotic resistance, much research has been focused on targeting S. aureus virulence factors, including toxins and biofilm-associated proteins, in an attempt to develop effective SAP therapeutics. Despite several promising leads, many hurdles still remain for S. aureus vaccine research. Here, we review the state-of-the-art SAP therapeutics, highlight their pitfalls, and discuss alternative approaches of potential significance and future perspectives.

Identification of secreted and surface proteins from Enterococcus faecalis

2009 ◽  
Vol 55 (8) ◽  
pp. 967-974 ◽  
Author(s):  
Abdellah Benachour ◽  
Thierry Morin ◽  
Laurent Hébert ◽  
Aurélie Budin-Verneuil ◽  
André Le Jeune ◽  
...  
Keyword(s):  
Cell Surface ◽  
Enterococcus Faecalis ◽  
Virulence Factors ◽  
Gel Electrophoresis ◽  
Ion Trap ◽  
Surface Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Proteomic Approach ◽  
Associated Proteins

Secreted and surface proteins of bacteria are key molecules that interface the cell with the environment. Some of them, corresponding to virulence factors, have already been described for Enterococcus faecalis , the predominant species involved in enterococcal nosocomial infections. In a global proteomic approach, the identification of the most abundant secreted and surface-associated proteins of E. faecalis JH2-2 strain was carried out. These proteins were separated by gel electrophoresis or directly subjected to in vivo trypsinolysis and then analyzed by liquid chromatography – electrospray ion trap tandem mass spectrometry. Putative functions were assigned by homology to the translated genomic database of E. faecalis. A total of 44 proteins were identified, eight secreted proteins from the supernatant culture and 38 cell surface proteins from two-dimensional gel electrophoresis and in vivo trypsinolysis among which two are common to the two groups. Their sequences analysis revealed that 35 of the 44 proteins harbour characteristic features (signal peptide or transmembrane domains) consistent with an extracellular localization. This study may be considered as an important step to encourage proteomic-based investigations of E. faecalis cell surface associated proteins that could lead to the discovery of virulence factors and to the development of new therapeutic tools.

scholarly journals The nucleoid-associated protein IHF acts as a “domainin” protein coordinating the bacterial virulence traits with global transcription

2020 ◽  
Author(s):  
Sylvie Reverchon ◽  
Sam Meyer ◽  
Raphaël Forquet ◽  
Florence Hommais ◽  
Georgi Muskhelishvili ◽  
...  
Keyword(s):  
Transcriptional Response ◽  
Dna Topology ◽  
Dickeya Dadantii ◽  
Genomic Expression ◽  
Environmental Signals ◽  
Virulence Traits ◽  
Associated Proteins ◽  
Response To Stress ◽  
Host Infection ◽  
First Time

AbstractBacterial pathogenic growth requires a swift coordination of pathogenicity functions with various kinds of environmental stresses encountered in the course of host infection. Among the factors critical for bacterial adaptation are changes of DNA topology and binding effects of nucleoid-associated proteins transducing the environmental signals to the chromosome and coordinating the global transcriptional response to stress. In this study we use the model phytopathogen Dickeya dadantii to analyse the organisation of transcription by the nucleoid-associated protein IHF. We determine both phenotypic effects of ihfA mutation on D. dadantii virulence and the transcriptional response under various conditions of growth. For the first time in enterobacteria, we examine the transcriptome of an IHF-depleted mutant under conditions of DNA relaxation, revealing a subtle interplay between IHF and DNA topology. We show that this mutation reorganises the genomic expression by altering the distribution of DNA supercoils along the chromosome at different length scales, thus affecting many virulence genes involved in both symptomatic and asymptomatic phases of infection, including those required for pectin catabolism. Altogether, we propose that IHF is a “domainin” protein, the inactivation of which impairs the coordination of chromosomal stress-response domains harbouring various virulence traits, thus abrogating the pathogenicity of D. dadantii.

Comparative secretome analyses of toxigenic and atoxigenic Rathayibacter species

2021 ◽  
Author(s):  
Matthew Tancos ◽  
Michael McMahon ◽  
Wesley Garrett ◽  
Douglas G Luster ◽  
Elizabeth Rogers
Keyword(s):  
Plant Pathogen ◽  
Plant Pathogens ◽  
Extracellular Proteins ◽  
Department Of Agriculture ◽  
Homologous Proteins ◽  
Diagnostic Assays ◽  
Animal Pathogens ◽  
Associated Proteins ◽  
Inspection Service ◽  
Related Proteins

Phytopathogenic Rathayibacter species are unique bacterial plant pathogens as they are obligately vectored by plant parasitic Anguinid nematodes to the developing seedheads of forage grasses and cereals. This understudied group of plant-associated Actinomycetes includes the neurotoxigenic plant pathogen, R. toxicus, which causes annual ryegrass toxicity in grazing livestock. Rathayibacter toxicus is currently endemic to Australia and is listed as a plant pathogen select agent by the U.S. Department of Agriculture – Animal and Plant Health Inspection Service. The complex Rathayibacter disease cycle requires intimate interactions with the nematode vector and plant hosts, which warrants an increased understanding of the secretory and surface-associated proteins that mediate these diverse eukaryotic interactions. Here we present the first comparative secretome analysis for this complex, nematode-vectored Rathayibacter genera that compares the three agronomically-damaging toxigenic and atoxigenic Rathayibacter species, R. toxicus, R. iranicus, and R. tritici. The exoproteomic comparison identified 1,423 unique proteins between the three species using LC-MS/MS, leading to the identification of putative pathogenicity-related proteins and proteins that may mediate nematode attachment. Of the uniquely identified proteins, 94 homologous proteins were conserved between the three Rathayibacter exoproteomes and comprised between 43.4 – 58.6% of total protein abundance. Comparative analyses revealed both conserved and uniquely expressed extracellular proteins, which, interestingly, had more similarities to extracellular proteins commonly associated with bacterial animal pathogens than classical plant pathogens. This comparative exoproteome analysis will facilitate the characterization of proteins essential for vector attachment and host colonization and assist in the development of serological diagnostic assays.

scholarly journals The Spl Serine Proteases Modulate Staphylococcus aureus Protein Production and Virulence in a Rabbit Model of Pneumonia

mSphere ◽  
2016 ◽  
Vol 1 (5) ◽  
Author(s):  
Alexandra E. Paharik ◽  
Wilmara Salgado-Pabon ◽  
David K. Meyerholz ◽  
Mark J. White ◽  
Patrick M. Schlievert ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Virulence Factors ◽  
Serine Proteases ◽  
Rabbit Model ◽  
Human Infection ◽  
Lung Damage ◽  
Wild Type ◽  
Content Type ◽  
Associated Proteins ◽  
Human Proteins

ABSTRACT Staphylococcus aureus is a versatile human pathogen that produces an array of virulence factors, including several proteases. Of these, six proteases called the Spls are the least characterized. Previous evidence suggests that the Spls are expressed during human infection; however, their function is unknown. Our study shows that the Spls are required for S. aureus to cause disseminated lung damage during pneumonia. Further, we present the first example of a human protein cut by an Spl protease. Although the Spls were predicted not to cut staphylococcal proteins, we also show that an spl mutant has altered abundance of both secreted and surface-associated proteins. This work provides novel insight into the function of Spls during infection and their potential ability to degrade both staphylococcal and human proteins. The Spl proteases are a group of six serine proteases that are encoded on the νSaβ pathogenicity island and are unique to Staphylococcus aureus. Despite their interesting biochemistry, their biological substrates and functions in virulence have been difficult to elucidate. We found that an spl operon mutant of the community-associated methicillin-resistant S. aureus USA300 strain LAC induced localized lung damage in a rabbit model of pneumonia, characterized by bronchopneumonia observed histologically. Disease in the mutant-infected rabbits was restricted in distribution compared to that in wild-type USA300-infected rabbits. We also found that SplA is able to cleave the mucin 16 glycoprotein from the surface of the CalU-3 lung cell line, suggesting a possible mechanism for wild-type USA300 spreading pneumonia to both lungs. Investigation of the secreted and surface proteomes of wild-type USA300 and the spl mutant revealed multiple alterations in metabolic proteins and virulence factors. This study demonstrates that the Spls modulate S. aureus physiology and virulence, identifies a human target of SplA, and suggests potential S. aureus targets of the Spl proteases. IMPORTANCE Staphylococcus aureus is a versatile human pathogen that produces an array of virulence factors, including several proteases. Of these, six proteases called the Spls are the least characterized. Previous evidence suggests that the Spls are expressed during human infection; however, their function is unknown. Our study shows that the Spls are required for S. aureus to cause disseminated lung damage during pneumonia. Further, we present the first example of a human protein cut by an Spl protease. Although the Spls were predicted not to cut staphylococcal proteins, we also show that an spl mutant has altered abundance of both secreted and surface-associated proteins. This work provides novel insight into the function of Spls during infection and their potential ability to degrade both staphylococcal and human proteins.

scholarly journals Cell-length heterogeneity: a population-level solution to growth/virulence trade-offs in the plant pathogen Dickeya dadantii

2019 ◽  
Vol 15 (8) ◽  
pp. e1007703 ◽  
Author(s):  
Zhouqi Cui ◽  
Ching-Hong Yang ◽  
Roshni R. Kharadi ◽  
Xiaochen Yuan ◽  
George W. Sundin ◽  
...  
Keyword(s):  
Plant Pathogen ◽  
Population Level ◽  
Cell Length ◽  
Dickeya Dadantii ◽  
Trade Offs

scholarly journals Genetic analysis of two phosphodiesterases reveals cyclic diguanylate regulation of virulence factors in Dickeya dadantii

2010 ◽  
Vol 77 (3) ◽  
pp. 787-800 ◽  
Author(s):  
Xuan Yi ◽  
Akihiro Yamazaki ◽  
Eulandria Biddle ◽  
Quan Zeng ◽  
Ching-Hong Yang
Keyword(s):  
Genetic Analysis ◽  
Virulence Factors ◽  
Cyclic Diguanylate ◽  
Dickeya Dadantii

Cyt toxin expression reveals an inverse regulation of insect and plant virulence factors of Dickeya dadantii

2010 ◽  
Vol 12 (12) ◽  
pp. 3290-3301 ◽  
Author(s):  
Denis Costechareyre ◽  
Bedis Dridi ◽  
Yvan Rahbé ◽  
Guy Condemine
Keyword(s):  
Virulence Factors ◽  
Dickeya Dadantii
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