Search results for "Virulence factor"

showing 10 items of 85 documents

N-acyl-homoserine-lactone quorum sensing in tomato phytopathogenic Pseudomonas spp. is involved in the regulation of lipodepsipeptide production

2012

Pseudomonas corrugata and Pseudomonas mediterranea are two closely related phytopathogenic bacteria both causal agents of tomato pith necrosis. P. corrugata produces phytotoxic and antimicrobial cationic lipodepsipeptides (LDPs) which are thought to act as major virulence factors. Previous studies have demonstrated that P. corrugata CFBP 5454 has an N-acyl homoserine lactone (AHL) quorum sensing (QS) system PcoI/PcoR and that LDP production occurs at high population densities. No molecular studies on virulence have thus far been reported for P. mediterranea. In this study, we show that P. mediterranea also produces LDPs as well as possessing an AHL-dependent QS system, designated PmeI/PmeR,…

Pseudomonas mediterraneaVirulence FactorsLipoproteinsPlant DiseaseHomoserineVirulenceBioengineeringBiologyAcyl-ButyrolactonesPseudomonaAcyl-ButyrolactoneApplied Microbiology and BiotechnologyTomatoMicrobiologychemistry.chemical_compoundSolanum lycopersicumVirulence FactorDepsipeptidesPseudomonasLycopersicon esculentumLipoproteinPromoter Regions GeneticDepsipeptidePlant DiseasesAntimicrobial Cationic PeptideVirulencePseudomonasGeneral MedicineLipodepsipeptidesbiology.organism_classificationPseudomonas corrugataQuorum sensingPseudomonas corrugataQuorum sensingN-Acyl homoserine lactonePhenotypechemistryPseudomonas mediterranea; Pseudomonas corrugata; Quorum sensing; Lipodepsipeptides; Virulence; TomatoMutationLipodepsipeptidePseudomonas mediterraneaBacteriaBiotechnologyAntimicrobial Cationic PeptidesJournal of Biotechnology
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Pdl1 Is a Putative Lipase that Enhances Photorhabdus Toxin Complex Secretion

2012

The Toxin Complex (TC) is a large multi-subunit toxin first characterized in the insect pathogens Photorhabdus and Xenorhabdus, but now seen in a range of pathogens, including those of humans. These complexes comprise three protein subunits, A, B and C which in the Xenorhabdus toxin are found in a 4∶1∶1 stoichiometry. Some TCs have been demonstrated to exhibit oral toxicity to insects and have the potential to be developed as a pest control technology. The lack of recognisable signal sequences in the three large component proteins hinders an understanding of their mode of secretion. Nevertheless, we have shown the Photorhabdus luminescens (Pl) Tcd complex has been shown to associate with th…

QH301-705.5Protein subunitImmunologyBacterial ToxinsMicrobiologiaXenorhabdusPathogenesisBiologymedicine.disease_causeMicrobiologyVirulence factorXenorhabdusMicrobiology03 medical and health sciencesBacterial ProteinsVirologyPhotorhabdus luminescensManducaGeneticsmedicineEscherichia coliGram NegativeAnimalsSecretionBiology (General)Molecular BiologyEscherichia coliBiologyMicrobial PathogensBacterial Secretion Systems030304 developmental biology0303 health sciences030306 microbiologyToxinMembrane ProteinsLipaseRC581-607biology.organism_classificationBacterial PathogensHost-Pathogen InteractionLarvaBacteris patògensParasitologyImmunologic diseases. AllergyPhotorhabdusProteïnesPhotorhabdusResearch ArticlePLoS Pathogens
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Salmonella bongori Provides Insights into the Evolution of the Salmonellae

2011

The genus Salmonella contains two species, S. bongori and S. enterica. Compared to the well-studied S. enterica there is a marked lack of information regarding the genetic makeup and diversity of S. bongori. S. bongori has been found predominantly associated with cold-blooded animals, but it can infect humans. To define the phylogeny of this species, and compare it to S. enterica, we have sequenced 28 isolates representing most of the known diversity of S. bongori. This cross-species analysis allowed us to confidently differentiate ancestral functions from those acquired following speciation, which include both metabolic and virulence-associated capacities. We show that, although S. bongori…

Salmonellamedicine.disease_causeSettore MED/42 - Igiene Generale E ApplicataTranslocation GeneticEnteropathogenic Escherichia coli1108 Medical MicrobiologySalmonellaCOMPLETE GENOME SEQUENCEIII SECRETION SYSTEMBiology (General)PATHOGENICITY ISLAND 2PhylogenyGenetics0303 health sciencesbiologyVirulenceEffectorPARASITOLOGYENTERICA SEROVAR TYPHIMURIUMSalmonella entericaGenomicsSalmonella bongori evolutionary genomicsBiological EvolutionUREIDOGLYCOLLATE LYASEInfectious DiseasesSalmonella enterica1107 ImmunologyQR180MedicineKLEBSIELLA-PNEUMONIAELife Sciences & BiomedicineResearch Article0605 MicrobiologySalmonella bongoriMICROBIOLOGYESCHERICHIA-COLI K-12Genomic IslandsQH301-705.5Sequence analysisVirulence FactorsImmunologyVirulenceVIROLOGYENCODED EFFECTORsalmonella; salmonella bongori; evoluzione geneticaMicrobiologyQH30103 medical and health sciencesVirologyGeneticsmedicineMICROARRAY ANALYSISAnimalsHumansEnteropathogenic Escherichia coliBiologyMolecular BiologyGene030304 developmental biologyEvolutionary BiologyScience & Technology030306 microbiologyANTIBIOTIC-RESISTANCESequence Analysis DNARC581-607biology.organism_classificationGenes BacterialImmunologic diseases. Allergy
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Host-Nonspecific Iron Acquisition Systems and Virulence in the Zoonotic Serovar of Vibrio vulnificus

2014

ABSTRACT The zoonotic serovar of Vibrio vulnificus (known as biotype 2 serovar E) is the etiological agent of human and fish vibriosis. The aim of the present work was to discover the role of the vulnibactin- and hemin-dependent iron acquisition systems in the pathogenicity of this zoonotic serovar under the hypothesis that both are host-nonspecific virulence factors. To this end, we selected three genes for three outer membrane receptors ( vuuA , a receptor for ferric vulnibactin, and hupA and hutR , two hemin receptors), obtained single and multiple mutants as well as complemented strains, and tested them in a series of in vitro and in vivo assays, using eels and mice as animal models. Th…

SerotypeVirulence FactorsSequence analysisIronImmunologyVirulenceVibrio vulnificusBiologyMicrobiologyMicrobiologyGene Knockout TechniquesMiceVibrio InfectionsAnimalsNatural reservoirOxazolesVibrio vulnificusGeneMice Inbred BALB CVirulenceGenetic Complementation TestMembrane Transport ProteinsBacterial Infectionsbiology.organism_classificationAmidesDisease Models AnimalInfectious DiseasesVibrio InfectionsHeminParasitologyBacterial outer membraneInfection and Immunity
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F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin

1994

The F17b fimbriae encoded by the transmissible virulence plasmid Vir, also coding for cytotoxic necrotizing factor type 2, were characterized. A 5.7-kb region of Vir mediates in vitro N-acetylglucosamine-sensitive adhesion to calf intestinal villi. Sequence analysis revealed that this region codes for a structural subunit and an adhesin closely related to the F17-A and F17-G proteins encoded by the F17 fimbrial gene cluster. The F17b-A gene presents an open reading frame of 540 bp encoding a polypeptide of 180 amino acids with a putative signal peptide of 21 residues. The mature protein shows an identity of 74% with the F17-A structural subunit. This 20-kDa protein is recognized by antiseru…

Signal peptideVirulence Factors[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataImmunologyFimbriaMutantBiologymedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsGene clusterEscherichia colimedicineAmino Acid SequenceEscherichia coliPeptide sequenceAdhesins Escherichia coliAntigens BacterialBase SequenceCytotoxinsEscherichia coli ProteinsSEQUENCE NULECOTIDIQUEbiochemical phenomena metabolism and nutritionMolecular biology[SDV] Life Sciences [q-bio]Bacterial adhesinOpen reading frameInfectious DiseasesFimbriae BacterialCLONAGE DE GENEParasitologyResearch ArticleBacterial Outer Membrane ProteinsPlasmidsInfection and Immunity
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Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis

2008

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolidesFEBS Letters
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Phenotypic and genotypic study on antibiotic resistance and pathogenic factors of Staphylococcus aureus isolates from small ruminant mastitis milk in…

2021

Staphyloccoccus aureus is the major cause of mastitis in small ruminants in the Mediterranean farms causing severe losses to dairy industry. Antibiotic treatment has been the most common approach to control these infections. Aim of this study was to investigate antimicrobial resistance (AMR), virulence factors and biofilm-related genes of 84 Sicilian strains of S. aureus isolated from sheep and goats milk during two different periods δT1 (2006-2009) and δT2 (2013-2015). Kirby Bauer method and Polymerase Chain Reaction (PCR) were utilized to monitor AMR and related genes (mecA, tetK, tetM, ermA, ermC). Moreover, toxin genes (tsst-1, sea-see, seg-sej, and sep) and biofilm genes (bap, ica, sas…

Staphylococcus aureusStaphylococcus aureus; Antimicrobial resistance; Virulence factors BiofilmVirulence factorsTetracyclineSulfamethoxazoleSCCmecBiofilmBiologyTP368-456medicine.disease_causemedicine.diseaseAntimicrobial resistanceFood processing and manufactureArticleMicrobiologyMastitisMultiple drug resistanceAntibiotic resistanceStaphylococcus aureusmedicineStaphylococcus aureuVancomycinFood Sciencemedicine.drugItalian Journal of Food Safety
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A Superantigen as Virulence Factor in an Acute Bacterial Infection

1994

This study addresses the role of a bacterial superantigen as a potential virulence factor during an acute systemic infection. BALB/c mice were intravenously infected with a recombinant Staphylococcus aureus strain capable of producing plasmid-encoded staphylococcal enterotoxin B (SEB) or with the SEB plasmid-deficient parental strain. Infection with SEB-producing bacteria resulted in an initial expansion and subsequent decrease of circulating V beta 8+ T lymphocytes. This numeric decrease was accompanied by a SEB-specific state of hyporesponsiveness of splenic T cells. In parallel with SEB-triggered unresponsiveness of a large proportion of T lymphocytes, a weakening of the overall T cell r…

T-LymphocytesT cellVirulencechemical and pharmacologic phenomenaEnterotoxinmedicine.disease_causeVirulence factorMicrobiologyEnterotoxinsMiceSuperantigenmedicineAnimalsImmunology and AllergyAntigens BacterialMice Inbred BALB CSuperantigensVirulencebiologyhemic and immune systemsT lymphocyteStaphylococcal Infectionsbiology.organism_classificationbiological factorsInfectious Diseasesmedicine.anatomical_structureOrgan SpecificityStaphylococcus aureusAcute DiseaseImmunologyBacteriaThe Journal of Infectious Diseases
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IMMUNOGENICITY OF AN ACELLULAR PERTUSSIS VACCINE COMPOSED OF GENETICALLY INACTIVATED PERTUSSIS TOXIN COMBINED WITH FILAMENTOUS HEMAGGLUTININ AND PERT…

1993

We studied the immunogenicity of an acellular pertussis vaccine composed of genetically detoxified pertussis toxin (PT-9K/129G), filamentous haemagglutinin, and a 69-kilodalton protein, pertactin, in 30 children aged 12 to 24 months and in 80 infants aged 2 to 4 months. A significant increase of the neutralizing titer and of the titers against pertussis toxin, filamentous hemagglutinin, and pertactin, as determined by enzyme-linked immunosorbent assay, was achieved after three doses of vaccine in all the children; a significant increase of these antibody titers was obtained in 100%, 96.1%, 93.5%, and 98.7% of the infants, respectively.

Time FactorsFilamentous haemagglutinin adhesinPertussis toxincomplex mixturesBordetella pertussisMicrobiologyNeutralization TestsHumansMedicineVirulence Factors BordetellaAdhesins BacterialImmunization ScheduleWhooping coughPertussis VaccineAntigens Bacterialbusiness.industryImmunogenicitypertussisAntibody titerInfantmedicine.diseaseAntibodies BacterialVirologyVaccinationTiterHemagglutininsPertussis ToxinVaccines InactivatedChild PreschoolImmunoglobulin GPediatrics Perinatology and Child HealthDrug EvaluationPertactinbusinessVaccinepertussis; VaccineBacterial Outer Membrane Proteins
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Effect of priming with diphtheria and tetanus toxoids combined with whole-cell pertussis vaccine or with acellular pertussis vaccine on the safety an…

1995

Objective: To evaluate the safety and the immunogenicity of a booster dose of recombinant acellular pertussis vaccine combined with diphtheria and tetanus toxoids (DTaP, Biocine SpA) in 15- to 21-month-old children primed in infancy with either whole-cell diphtheria-tetanus-pertussis (DTwP) vaccine or DTaP vaccine. Design: Open-label second phase of a double-masked, controlled trail, with masked analysis of serum samples. Participants and setting: Three hundred fifty children, 15 to 21 months of age, who had been primed at 2, 4, and 6 months of age with either three doses of DTaP vaccine (n = 173) or DTwP vaccine (n = 177). The children were enrolled in eight vaccination centers in Italy. I…

Time FactorsWhooping CoughImmunization SecondaryEnzyme-Linked Immunosorbent AssayBooster dosecomplex mixturesBordetella pertussisDouble-Blind MethodmedicineHumansVirulence Factors BordetellaDiphtheria-Tetanus-Pertussis VaccineWhooping coughPertussis VaccineVaccines SyntheticTetanusbusiness.industryDiphtheriaToxoidAntibody titerInfantmedicine.diseaseAntibodies BacterialVirologyVACCINE pertussisVaccinationPertussis ToxinPediatrics Perinatology and Child HealthImmunologyPertussis vaccinebusinessFollow-Up Studiesmedicine.drug
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