0000000000350422

AUTHOR

Andrei Soliakov

showing 3 related works from this author

Alhydrogel® adjuvant, ultrasonic dispersion and protein binding: A TEM and analytical study

2011

Aluminium-based vaccine adjuvants have been in use since the 1920s. Aluminium hydroxide (alum) that is the chemical basis of Alhydrogel, a widely used adjuvant, is a colloid that binds proteins to the particular surface for efficient presentation to the immune system during the vaccination process. Using conventional TEM and cryo-TEM we have shown that Alhydrogel can be finely dispersed by ultrasonication of the aqueous suspension. Clusters of ultrasonicated aluminium hydroxide micro-fibre crystals have been produced (∼ 10-100 nm), that are significantly smaller than those present the untreated Alhydrogel (∼ 2-12 μm). However, even prolonged ultrasonication did not produce a homogenous susp…

Sonicationmedicine.medical_treatmentGeneral Physics and Astronomychemistry.chemical_elementAluminum Hydroxidecomplex mixturesSuspension (chemistry)SonicationColloidchemistry.chemical_compoundAdjuvants ImmunologicMicroscopy Electron TransmissionStructural BiologyAluminiumparasitic diseasesmedicineGeneral Materials ScienceAntigensChemistryAlumAluminium hydroxideProteinsCell BiologyNegative stainCrystallographyChemical engineeringAdjuvantProtein BindingMicron
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Recombinant anthrax protective antigen: Observation of aggregation phenomena by TEM reveals specific effects of sterols.

2017

Abstract Negatively stained transmission electron microscope images are presented that depict the aggregation of recombinant anthrax protective antigen (rPA83 monomer and the PA63 prepore oligomer) under varying in vitro biochemical conditions. Heat treatment (50 °C) of rPA83 produced clumped fibrils, but following heating the PA63 prepore formed disordered aggregates. Freeze-thaw treatment of the PA63 prepore generated linear flexuous aggregates of the heptameric oligomers. Aqueous suspensions of cholesterol microcrystals were shown to bind small rPA83 aggregates at the edges of the planar bilayers. With PA63 a more discrete binding of the prepores to the crystalline cholesterol bilayer ed…

0301 basic medicineModels MolecularHot TemperatureBacterial ToxinsGeneral Physics and AstronomyFibrilOligomerNegative Staining03 medical and health scienceschemistry.chemical_compoundProtein AggregatesMicroscopy Electron TransmissionStructural BiologyFreezingGeneral Materials ScienceAntigens BacterialAqueous solutionChemistryBilayerCell BiologyHydrogen-Ion ConcentrationNegative stainSterolRecombinant ProteinsCrystallographySterols030104 developmental biologyMonomerCholesterolTransmission electron microscopyCrystallizationDeoxycholic AcidMicron (Oxford, England : 1993)
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The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states

2010

Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism. Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa). The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins. Short polymers often form circles, presumably by DSE. We also provide the first images of proteins bound to alhydrogel adjuvant. Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.

Models MolecularProtein FoldingPolymersVirulence FactorsYersinia pestismedicine.medical_treatmentVirulence factorMicrobiologychemistry.chemical_compoundProtein structureAdjuvants ImmunologicBacterial ProteinsMicroscopy Electron TransmissionmedicineProtein Structure QuaternaryBacterial Capsuleschemistry.chemical_classificationAntigens BacterialPlaguePlague VaccineGeneral VeterinaryGeneral Immunology and MicrobiologybiologyPublic Health Environmental and Occupational HealthHemocyaninPolymerbiology.organism_classificationInfectious DiseasesMonomerYersinia pestischemistryBiophysicsMolecular MedicinePlague vaccineProtein foldingVaccine
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