Search results for "toxins"

showing 10 items of 799 documents

Role of iron, capsule, and toxins in the pathogenicity of Vibrio vulnificus biotype 2 for mice

1994

The virulence mechanisms of Vibrio vulnificus biotype 2 have been studied and compared with those of biotype 1 in mice as the experimental animals. Biotype 2 isolates from European eels were as virulent for mice as biotype 1 strains (50% lethal dose, about 10(5) CFU per mouse); a septicemic infection developed in less than 24 h. These strains had several properties in common with biotype 1 organisms including capsule expression, uptake of various iron sources, and production of exoproteins, whose role in mouse virulence has been demonstrated. We also discuss the implication of biotype 2 strains in human infections.

Blood Bactericidal ActivityIronImmunologyExotoxinsVirulenceVibrio vulnificusIn Vitro Techniquesmedicine.disease_causeMicrobiologyMicrobiologyMiceSpecies SpecificityVibrionaceaeVibrio InfectionsmedicineAnimalsHumansVibrioEelsVirulencebiologyToxinLethal dosebiology.organism_classificationVibrioBacterial Typing TechniquesInfectious DiseasesVibrio InfectionsParasitologyBacteriaResearch ArticleInfection and Immunity
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Demonstration of High-Affinity Binding Sites for C3a Anaphylatoxin on Guinea-Pig Platelets

1978

3H-serotonin release from guinea-pig platelets was demonstrated to be the consequence of C3a binding to these cells. A Scatchard analysis of dose-response data of the 125I-C3a binding pattern to guinea-pig platelets pointed to the existence of binding sites with high and low affinity for the C3a molecule (HA and LA receptors). HA receptors are specific for C3a with intact C-terminal arginine. whereas C3adesarg only interacts with LA receptors. The release of serotonin may be induced by a combined reaction of C3a with HA receptors and LA receptors on the platelet membrane.

Blood PlateletsAnaphylatoxinsSerotoninBinding SitesArginineChemistryGuinea PigsImmunologyTemperaturechemical and pharmacologic phenomenaCarboxypeptidasesComplement C3General MedicineGuinea pigBiochemistryAnimalsProtease-activated receptorPlateletAnaphylatoxinSerotoninBinding sitePeptidesReceptorScandinavian Journal of Immunology
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Comparative study on biological activities of various anaphylatoxins (C4a, C3a, C5a)

1981

Several anaphylatoxic substances (human C3a, guinea pig C3a, human C4a, guinea pig C5a, and a synthetic C3a-related hexapeptide) were compared with regard to their ability to induce secretion of [3H] serotonin from guinea pig platelets. Functional identity of the C3a preparations, C4a, and the hexapeptide was demonstrated by the phenomenon of crossed desensitization. Whereas C3a of human and guinea pig origin proved to be qualitatively and quantitatively identical, C4a expressed only 3% of the activity of the C3 fragments on a molar basis. Investigations with goat anti-guinea pig C3a demonstrate that human and guinea pig C3a possess one antigenic determinant in common; however, this determi…

Blood PlateletsAnaphylatoxinsSerotoninGuinea PigsImmunologyComplement C5achemical and pharmacologic phenomenaGuinea pigThrombinmedicineAnimalsHumansImmunology and AllergyPlateletAnaphylatoxinSecretionChemistryImmune SeraThrombinComplement C4aComplement C5Complement C4Biological activityComplement C3Complement System ProteinsIn vitroBiochemistryComplement C3aSerotoninPeptidesmedicine.drugInflammation
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Platelet Activation: a New Biological Activity of Guinea-pig C3a Anaphylatoxin

1978

3H-serotonin-release from labelled gp-platelets is established as a sensitive method for testing a new biological activity of gp-C3a anaphylatoxin in an autologous situation. Time-, dose- and temperature-dependent release reactions as well as specific inhibition by carboxypeptidase B and anti-C3a antibodies show that C3a is a potent and specific inducer of platelet activation. Inactive C3a does not induce 3H-serotonin-release but specifically inhibits the action of C3a on platelets.

Blood PlateletsAnaphylatoxinsSerotoninTime FactorsGuinea PigsImmunologychemical and pharmacologic phenomenaTritiumGuinea pigComplement Inactivator ProteinsAnimalsPlateletAnaphylatoxinInducerPlatelet activationComplement Inactivator ProteinsbiologyChemistryTemperatureBiological activityComplement C3General MedicineChromium RadioisotopesBiochemistrybiology.proteinAntibodyPeptidesScandinavian Journal of Immunology
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Comparative study on biological effects of the guinea pig complement-peptide C3a and C3a-related synthetic oligopeptides

1980

Dose-response experiments with guinea pig C3a and a synthetic hexapeptide (amino acid residues 72–77), representing the COOH-terminal sequence of human C3a, were performed in two recently described bioassay systems for C3a, i.e. cytotoxicity against tumor cells measured as LDH and 51Cr-release and non cytolytic serotonin release from guinea pig platelets. Compared to the classical anaphylatoxic assay (guinea pig ileum contraction), nearly identical reactivities were observed in all three test systems with C3a and, although quantitatively different, with hexapeptide.

Blood PlateletsCytotoxicity ImmunologicAnaphylatoxinsSerotoninContraction (grammar)ImmunologyDose-Response Relationship Immunologicchemical and pharmacologic phenomenaPeptideBiologyGuinea pigMiceAnimalsBioassayPlateletCytotoxicityMolecular Biologychemistry.chemical_classificationOligopeptideL-Lactate DehydrogenaseComplement C3Peptide Chain Termination TranslationalCytolysisBiochemistrychemistryBiological AssayOligopeptidesMolecular Immunology
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Isolation and toxicity of Bacillus thuringiensis from potato-growing areas in Bolivia

2004

Bacillus thuringiensis was isolated from 116 samples collected in high altitude potato-growing areas in Bolivia. In these regions, main potato pests are the potato tuberworm Phthorimaea operculella, and the Andean weevils Premnotrypes latithorax and Rhigopsidius tucumanus. B. thuringiensis was found in 60% of the samples. The main percentage of samples with B. thuringiensis was found in larvae of R. tucumanus (78%). Bioassays were performed with 112 isolates. None resulted toxic to either larvae or adults of the two Andean weevils. However, 18 isolates from this study showed more toxicity against the beet armyworm Spodoptera exigua than the standard strain var. kurstaki isolated from DELFIN…

BoliviaVeterinary medicineBacterial ToxinsBacillus thuringiensisPolymerase Chain ReactionBacterial ProteinsBeet armywormBacillus thuringiensisExiguaBotanyAnimalsSoil MicrobiologyEcology Evolution Behavior and SystematicsSolanum tuberosumbiologyfungiDustbiology.organism_classificationGelechiidaePhthorimaea operculellaLepidopteraBiopesticideLarvaWeevilsElectrophoresis Polyacrylamide GelRestriction fragment length polymorphismPolymorphism Restriction Fragment LengthSolanaceaeJournal of Invertebrate Pathology
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Preoperative preparation of «loss of domain» hernia. Progressive pneumoperitoneum and botulinum toxin type A.

2017

Preoperative progressive pneumoperitoneum and botulinum toxin type A are useful tools in the preparation of patients with loss of domain hernias. Both procedures are complementary in the surgical repair, especially with the use of prosthetic techniques without tension, that allow a integral management of these patients. The aim of this paper is to update concepts related to both procedures, emphasizing the advantages that take place in the preoperative management of loss of domain hernias.

Botulin toxinmedicine.medical_specialtyIncisional hernia030230 surgeryDomain (software engineering)03 medical and health sciences0302 clinical medicinePneumoperitoneumPreoperative CareMedicineHumansHerniaBotulinum Toxins Type ASurgical repairbusiness.industryGeneral Engineeringmedicine.diseaseBotulinum toxinSurgeryHernia Abdominal030220 oncology & carcinogenesisAnesthesiabusinessPneumoperitoneum Artificialmedicine.drugBotulinum toxin typeCirugia espanola
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Shared Binding Sites for the Bacillus thuringiensis Proteins Cry3Bb, Cry3Ca, and Cry7Aa in the African Sweet Potato Pest Cylas puncticollis (Brentida…

2014

ABSTRACT Bacillus thuringiensis Cry3Bb, Cry3Ca, and Cry7Aa have been reported to be toxic against larvae of the genus Cylas , which are important pests of sweet potato worldwide and particularly in sub-Saharan Africa. However, relatively little is known about the processing and binding interactions of these coleopteran-specific Cry proteins. The aim of the present study was to determine whether Cry3Bb, Cry3Ca, and Cry7Aa proteins have shared binding sites in Cylas puncticollis to orient the pest resistance strategy by genetic transformation. Interestingly, processing of the 129-kDa Cry7Aa protoxin using commercial trypsin or chymotrypsin rendered two fragments of about 70 kDa and 65 kDa. N-…

Brush borderBacillus thuringiensisBiological pest controlHemolysin ProteinsApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEnvironmental MicrobiologymedicineAnimalsIpomoea batatasBinding sitePlant DiseasesBinding SitesChymotrypsinBacillus thuringiensis ToxinsEcologybiologyfungiTrypsinbiology.organism_classificationColeopteraEndotoxinsLarvabiology.proteinPEST analysisFood ScienceBiotechnologymedicine.drugApplied and Environmental Microbiology
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Immunohistochemical Detection of Binding of Cryia Crystal Proteins of Bacillus thuringiensis in Highly Resistant Strains of Plutella xylostella (L.) …

1995

We detected binding of insecticidal crystal proteins from Bacillus thuringiensis in one susceptible strain and six resistant strains of diamondback moth, Plutella xylostella, from Hawaii. Immunohistochemical tests with tissue sections from larval midguts showed specific binding of CryIA(a), CryIA(b), and CryIA(c) to brush border membranes. CryIE, which is not toxic to P. xylostella, did not bind to midgut tissues. Larvae from one of the resistant strains ingested extremely high concentrations of a commercial formulation containing the three CryIA proteins without suffering midgut cell damage or mortality. This same resistant strain had previously been found to have greatly reduced binding o…

Brush borderBacterial ToxinsBacillus thuringiensisBiophysicsMothsHemolysin ProteinsBiochemistryEpitheliumHawaiiInsecticide ResistanceHemolysin ProteinsBacterial ProteinsIn vivoBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyDiamondback mothBacillus thuringiensis ToxinsMicrovillibiologyStrain (chemistry)fungiPlutellaMidgutCell Biologybiology.organism_classificationImmunohistochemistryMolecular biologyEndotoxinsLarvaBiochemical and Biophysical Research Communications
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Selective inhibition of binding of Bacillus thuringiensis Cry1Ab toxin to cadherin-like and aminopeptidase proteins in brush-border membranes and dis…

2007

Binding analyses with denatured epithelial membrane proteins from Bt (Bacillus thuringiensis) demonstrated at least two kinds of proteins, APNs (aminopeptidases N) and cadherin-like proteins, as possible receptors for the Cry1A class of Bt toxins. Two alternative models have been proposed, both based on initial toxin binding to a cadherin-like protein, but one involving APN and the other not. We have used two Bombyx mori strains (J65 and Kin), which are highly susceptible to Cry1Ab, to study the role of these two types of receptors on Cry1Ab toxin binding and cytotoxicity by means of the inhibitory effect of antibodies. BBMVs (brush-border membrane vesicles) of strain J65 incubated with lab…

Brush borderBacterial ToxinsBacillus thuringiensisCD13 Antigensmedicine.disease_causeBiochemistryAminopeptidaseAminopeptidasesAntibodiesHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsIntestinal MucosaReceptorMolecular BiologyMembranesbiologyBacillus thuringiensis ToxinsMicrovilliCadherinToxinfungiEpithelial CellsCell Biologybiology.organism_classificationBombyxMolecular biologyEndotoxinsMembrane proteinBiochemistrybiology.proteinBiological AssayAntibodyProtein BindingThe Biochemical journal
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