Search results for "RTX toxin"

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Early steps in the European eel (Anguilla anguilla)–Vibrio vulnificus interaction in the gills: Role of the RtxA13 toxin

2015

Vibrio vulnificus is an aquatic gram-negative bacterium that causes a systemic disease in eels called warm-water vibriosis. Natural disease occurs via water born infection; bacteria attach to the gills (the main portal of entry) and spread to the internal organs through the bloodstream, provoking host death by haemorrhagic septicaemia. V.vulnificus produces a toxin called RtxA13 that hypothetically interferes with the eel immune system facilitating bacterial invasion and subsequent death by septic shock. The aim of this work was to study the early steps of warm-water vibriosis by analysing the expression of three marker mRNA transcripts related to pathogen recognition (tlr2 and tlr5) and in…

GillsGillendocrine systemanimal structuresHost-pathogen relationshipBacterial ToxinsVibrio vulnificusAquatic ScienceBiologymedicine.disease_causertxA13MicrobiologyFish DiseasesImmune systemmedicineAnimalsEnvironmental ChemistryRNA MessengerImmune responseVibrio vulnificusPathogenToxinRTX toxinGeneral MedicineAnguillabiology.organism_classificationAcquired immune systemTLR2Gene Expression RegulationEuropean eelVibrio InfectionsChemokinesFish & Shellfish Immunology
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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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