Search results for "Hemolysin"

showing 9 items of 169 documents

Putative identification of an amphipathic alpha-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation.

2008

Abstract Escherichia coli hemolysin is a pore-forming protein belonging to the RTX toxin family. Cysteine scanning mutagenesis was performed to characterize the putative pore-forming domain of the molecule. A single cysteine residue was introduced at 48 positions within the sequence spanning residues 170–400 and labeled with the polarity-sensitive dye badan. Spectrofluorimetric analyses indicated that several amino acids in this domain are inserted into the lipid bilayer during pore formation. An amphipathic α-helix spanning residues 272–298 was identified that may line the aqueous pore. The importance of this sequence was highlighted by the introduction of two prolines at positions 284 and…

StereochemistryClinical BiochemistryAmino Acid MotifsPorinsmedicine.disease_causeBiochemistryProtein Structure SecondaryHemolysin ProteinsCell Line TumormedicineAnimalsHumansLipid bilayerMolecular BiologyEscherichia colichemistry.chemical_classificationEscherichia coli ProteinsRTX toxinMutagenesisErythrocyte MembraneHemolysinTransmembrane proteinAmino acidchemistryMutant ProteinsRabbitsCysteineBiological chemistry
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Potential of the Bacillus thuringiensis Toxin Reservoir for the Control of Lobesia botrana (Lepidoptera: Tortricidae), a Major Pest of Grape Plants▿

2006

ABSTRACT The potential of Bacillus thuringiensis Cry proteins to control the grape pest Lobesia botrana was explored by testing first-instar larvae with Cry proteins belonging to the Cry1, Cry2, and Cry9 groups selected for their documented activities against Lepidoptera. Cry9Ca, a toxin from B. thuringiensis , was the protein most toxic to L. botrana larvae, followed in decreasing order by Cry2Ab, Cry1Ab, Cry2Aa, and Cry1Ia7, with 50% lethal concentration values of 0.09, 0.1, 1.4, 3.2, and 8.5 μg/ml of diet, respectively. In contrast, Cry1Fa and Cry1JA were not active at the assayed concentration (100 μg/ml). In vitro binding and competition experiments showed that none of the toxins teste…

Tortricidaeanimal structuresBacterial ToxinsBacillus thuringiensisGenetically modified cropsMothsmedicine.disease_causeLobesia botranaApplied Microbiology and BiotechnologyLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsLobesia botranaBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsVitisPest Control BiologicalCry proteinsPlant DiseasesEcologybiologyBacillus thuringiensis ToxinsToxinbusiness.industryfungiPest controlfood and beveragesbiology.organism_classificationPlants Genetically ModifiedEndotoxinsHorticultureLarvaPEST analysisbusinessFood ScienceBiotechnology
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Staphylococcus aureus alpha toxin mediates polymorphonuclear leukocyte-induced vasocontraction and endothelial dysfunction.

2002

The effect of Staphylococcus aureus alpha toxin (alpha-toxin) on selectin-mediated neutrophil adhesion was investigated in polymorphonuclear leukocyte- (PMN) induced vasocontraction and endothelial dysfunction. Adherence of human PMNs to rat aortic endothelium increased significantly following stimulation of the endothelium with alpha-toxin (0.1, 0.5, and 1 microg/mL). This effect could be significantly attenuated by monoclonal antibodies directed against P-selectin or fucoidin, a carbohydrate known to block selectins. Unstimulated human PMNs (10(6)cells/mL) were added to organ chambers containing rat aortic rings stimulated with alpha-toxin (0.5 microg/mL). PMNs elicited a significant vaso…

Vascular smooth muscleEndotheliumNeutrophilsBacterial ToxinsPharmacologyBiologyIn Vitro TechniquesCritical Care and Intensive Care MedicineMicrocirculationHemolysin ProteinsFibrinolytic AgentsmedicineCell AdhesionAnimalsHumansEndothelial dysfunctionStaphylococcus aureus alpha toxinAortaThrombinAzepinesTriazolesmedicine.diseaseRatsmedicine.anatomical_structureVasoconstrictionImmunologyEmergency MedicineEndothelium Vascularmedicine.symptomVasoconstrictionSelectinBlood vesselShock (Augusta, Ga.)
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Pathogenicity of live bacteria and extracellular products of motileAeromonasisolated from eels

1995

The pathogenic activities in vitro and in vivo of live bacteria and extracellular products (ECP) of 24 motile Aeromonas strains were investigated. Most Aer. hydrophila and Aer. jandaei isolates were pathogenic for eels (LD50 105·4‐107·6 cfu fish‐1) but no Aer. sobria, Aer. caviae and Aer. allosaccharophila caused mortality in eels at doses of > 108·4 cfu fish‐1. Of these Aeromonas strains, Aer. hydrophila and Aer. jandaei in particular produced elastases and haemolysins against fish erythrocytes. ECP from Aer. hydrophila and Aer. jandaei caused degenerative changes in fish cell lines and were strongly toxic for eels (LD50 1·0–3·2 μg (g fish)‐1) reproducing the symptoms associated with natur…

animal structuresendocrine system diseasesbiologyToxinVirulenceHemolysinurologic and male genital diseasesmedicine.disease_causebiology.organism_classificationApplied Microbiology and BiotechnologyMicrobiologyMicrobiologyAeromonasVibrionaceaemedicineExtracellularhuman activitiesBacteriaExotoxinJournal of Applied Bacteriology
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The genotypes and virulence attributes of C. albicans isolates from oral leukoplakia

2021

Background There is a debate as to whether some types of oral leucoplakias (OL) are caused by Candida species, and whether they contribute to the malignant transformation, associated with a minority of such lesions. As no detailed population analysis of yeast isolates from OL is available, we evaluated the virulence attributes, and genotypes of 35 C. albicans from OL, and compared their genotypes with 18 oral isolates from healthy individuals. Material and Methods The virulence traits evaluated were esterase, phospholipase, proteinase, haemolysin and coagulase production, and phenotypic switching activity, and yeast adherence and biofilm formation. DNA from OL and control yeasts were evalua…

audio-visual resourcesGenotypePopulationPhenotypic switchingVirulenceBiologyEsterasepatient educationMicrobiologyGenotypeCandida albicansHumanseducationGeneral DentistryUNESCO:CIENCIAS MÉDICASCandidaeducation.field_of_studyOral Medicine and PathologyVirulenceResearchHemolysinoral cancerdiagnostic delayspanishCorpus albicansOtorhinolaryngologySurgeryinternetCoagulaseLeukoplakia OralMedicina Oral, Patología Oral y Cirugía Bucal
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Unshared binding sites for Bacillus thuringiensis Cry3Aa and Cry3Ca proteins in the weevil Cylas puncticollis (Brentidae)

2016

Bacillus thuringiensis Cry3Aa and Cry3Ca proteins have been reported to be toxic against the African sweetpotato pest Cylas puncticollis. In the present work, the binding sites of these proteins in C. puncticollis brush border vesicles suggest the occurrence of different binding sites, but only one of them is shared. Our results suggest that pest resistance mediated by alteration of the shared Cry-receptor binding site might not render both Cry proteins ineffective.

endocrine systemAfrican sweetpotato weevilBacillus thuringiensis ToxinsShort CommunicationBinding sitesInsect controlfungiBacillus thuringiensisToxicologyBinding CompetitiveInsect resistance managementEndotoxinsHemolysin ProteinsInsecticidal proteinsBacterial ProteinsAnimalsWeevilsToxicon
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Extent of variation of the Bacillus thuringiensis toxin reservoir: the case of the geranium bronze, Cacyreus marshalli butler (Lepidoptera: Lycaenida…

2002

ABSTRACT Despite the fact that around 200 cry genes from Bacillus thuringiensis have already been cloned, only a few Cry proteins are toxic towards a given pest. A crucial step in the mode of action of Cry proteins is binding to specific sites in the midgut of susceptible insects. Binding studies in insects that have developed cross-resistance discourage the combined use of Cry proteins sharing the same binding site. If resistance management strategies are to be implemented, the arsenal of Cry proteins suitable to control a given pest may be not so vast as it might seem at first. The present study evaluates the potential of B. thuringiensis for the control of a new pest, the geranium bronze…

endocrine systemBacterial ToxinsBacillus thuringiensisZoologymedicine.disease_causeApplied Microbiology and BiotechnologyBinding CompetitiveLepidoptera genitaliaHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanymedicineInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalBinding SitesEcologybiologyBacillus thuringiensis ToxinsToxinGeranium bronzefungiLycaenidaeMidgutPlantsbiology.organism_classificationEndotoxinsLepidopteraPEST analysisFood ScienceBiotechnologyApplied and environmental microbiology
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Dissimilar Regulation of Antimicrobial Proteins in the Midgut of Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Toxins or Baculoviru…

2015

Antimicrobial peptides (AMPs) and lysozymes are the main effectors of the insect immune system, and they are involved in both local and systemic responses. Among local responses, midgut immune reaction plays an important role in fighting pathogens that reach the insect body through the oral route, as do many microorganisms used in pest control. Under this point of view, understanding how insects defend themselves locally during the first phases of infections caused by food-borne pathogens is important to further improve microbial control strategies. In the present study, we analyzed the transcriptional response of AMPs and lysozymes in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae…

media_common.quotation_subjectAntimicrobial peptidesMolecular Sequence DataBacillus thuringiensislcsh:MedicineInsectSpodopteraSpodopteraMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaHemolymphAnimalsAmino Acid SequencePest Control Biologicallcsh:SciencePhylogenymedia_commonMultidisciplinarybiologyBacillus thuringiensis ToxinsSequence Homology Amino AcidMonophenol Monooxygenasefungilcsh:RMidgutbiology.organism_classificationEndotoxinsSettore AGR/11 - ENTOMOLOGIA GENERALE E APPLICATALarvaNoctuidaeInsect ProteinsMuramidaselcsh:QBaculoviridaeDigestive SystemAntimicrobial Cationic PeptidesResearch ArticlePLoS ONE
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Binding analysis of Bacillus thuringiensis Cry1 proteins in the sugarcane borer, Diatraea saccharalis (Lepidoptera: Crambidae).

2015

Sugarcane borer (Diatraea saccharalis, F.) is an important corn pest in South America and United States. The aim of the present study was to analyze the susceptibility and binding interactions of three Cry1A proteins and Cry1Fa in a Brazilian D. saccharalis population. The results showed that Cry1Ab was the most active, followed by Cry1Ac, Cry1Fa and Cry1Aa. All Cry1-biotinylated proteins tested bound specifically to the D. saccharalis brush border membrane vesicles (BBMV). Heterologous competition assays showed shared binding sites for all Cry1A proteins and another one shared by Cry1Fa and Cry1Ab. Thus, pyramiding Cry1Aa/Cry1Ac and Cry1F proteins would be a recommended strategy for managi…

media_common.quotation_subjectPopulationBacillus thuringiensisBiologyMothsDiatraea saccharalisCompetition (biology)Lepidoptera genitaliaInsecticide ResistanceHemolysin ProteinsCrambidaeBacterial ProteinsBacillus thuringiensisBotanyAnimalseducationPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commoneducation.field_of_studyBacillus thuringiensis Toxinsfungifood and beveragesbiology.organism_classificationEndotoxinsCry1AcPEST analysisJournal of invertebrate pathology
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