Search results for "BORRELIA"

showing 10 items of 78 documents

Structure of an outer surface lipoprotein BBA64 from the Lyme disease agent Borrelia burgdorferi which is critical to ensure infection after a tick b…

2013

Lyme disease is a tick-borne infection caused by the transmission of Borrelia burgdorferi from infected Ixodes ticks to a mammalian host during the blood meal. Previous studies have shown that the expression of B. burgdorferi surface-localized lipoproteins, which include BBA64, is up-regulated during the process of tick feeding. Although the exact function of BBA64 is not known, this lipoprotein is critical for the transmission of the spirochete from the tick salivary glands to the mammalian organism after a tick bite. Since the mechanism of development of the disease and the functions of the surface lipoproteins associated with borrel­iosis are still poorly understood, the crystal structur…

Models MolecularAntigens BacterialLyme DiseasebiologyIxodesTransmission (medicine)General MedicineTickbacterial infections and mycosesbiology.organism_classificationmedicine.diseaseMicrobiologyPathogenesisLyme diseaseX-Ray DiffractionStructural BiologyBorrelia burgdorferiSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationmedicineAnimalsIxodesBorrelia burgdorferiFunction (biology)LipoproteinActa crystallographica. Section D, Biological crystallography
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Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi.

2019

Lyme disease is an infection caused by the spirochete Borrelia burgdorferi after it is transmitted to a mammalian organism during a tick blood meal. B. burgdorferi encodes at least 140 lipoproteins located on the outer or inner membrane, thus facing the surroundings or the periplasmic space, respectively. However, most of the predicted lipoproteins are of unknown function, and only a few proteins are known to be essential for the persistence and virulence of the pathogen. One such protein is the periplasmic BB0323, which is indispensable for B. burgdorferi to cause Lyme disease and the function of which is associated with cell fission and outer membrane integrity. After expression and trans…

Models MolecularLyme DiseaseVirulence FactorsLipoproteinsVirulencePeriplasmic spaceBiologybiology.organism_classificationVirulence factorCell biologyBacterial ProteinsStructural BiologyBorrelia burgdorferiInner membraneSpectrinAmino Acid SequenceBorrelia burgdorferiBacterial outer membranePathogenActa crystallographica. Section D, Structural biology
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Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi

2014

Borrelia burgdorferi, the causative agent of Lyme disease is transmitted to the mammalian host organisms by infected Ixodes ticks. Transfer of the spirochaetal bacteria from Ixodes ticks to the warm-blooded mammalian organism provides a challenge for the bacteria to adapt and survive in the different environmental conditions. B. burgdorferi has managed to differentially express genes in response to the encountered changes such as temperature and pH variance or metabolic rate to survive in both environments. In recent years, much interest has been turned on genes that are upregulated during the borrelial transfer to mammalian organisms as this could reveal the proteins important in the patho…

Models MolecularMolecular Sequence DataSequence alignmentCrystallography X-RayMicrobiologyMicrobiologyLyme diseasemedicineAnimalsAmino Acid SequenceBorrelia burgdorferiGeneAntigens BacterialLyme DiseaseIxodesbiologyProtein superfamilybiology.organism_classificationmedicine.diseasePhenotypeInfectious DiseasesMembrane proteinBorrelia burgdorferiInsect ScienceParasitologyIxodesSequence AlignmentBacterial Outer Membrane ProteinsTicks and Tick-borne Diseases
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Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.

2013

Borrelia burgdorferi, which is the causative agent of Lyme disease, is transmitted from infected Ixodes ticks to a mammalian host following a tick bite. Upon changing the host organism from an Ixodes tick to a warm-blooded mammal, the spirochete must adapt to very different conditions, which is achieved by altering the expression of several genes in response to a changing environment. Recently, considerable attention has been devoted to several outer surface proteins, including BBA73, that undergo dramatic upregulation during the transmission of B. burgdorferi from infected Ixodes ticks to mammals and that are thought to be important for the establishment and maintenance of the infection. T…

Models MolecularMolecular Sequence DataStatic ElectricityBiophysicsCrystallography X-RayBiochemistryProtein Structure SecondaryMicrobiologyProtein structureAnimalsAmino Acid SequenceBorrelia burgdorferiCloning MolecularProtein Structure QuaternaryMolecular BiologyPeptide sequenceLyme DiseaseBinding SitesbiologyIxodesSequence Homology Amino AcidCell BiologyProtein superfamilyLigand (biochemistry)biology.organism_classificationSolutionsMembrane proteinBorrelia burgdorferiLyme disease microbiologyIxodesProtein MultimerizationBacterial Outer Membrane ProteinsBiochemical and biophysical research communications
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Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

2020

Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia tunicate outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. This article is protected …

Models MolecularProtein Conformation alpha-HelicalProtein familyLipoproteinsGenetic VectorsGene ExpressionPeptideBiochemistryMicrobiologyPathogenesis03 medical and health sciencesLyme diseaseStructural BiologyBorreliamedicineEscherichia coliHumansProtein Interaction Domains and MotifsAmino Acid SequenceBorrelia burgdorferiCloning MolecularMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseasebiologySequence Homology Amino AcidBorrelia030302 biochemistry & molecular biologybacterial infections and mycosesbiology.organism_classificationmedicine.diseaseRecombinant ProteinsProtein Structure TertiaryOuter surface proteinchemistryBorrelia burgdorferiProtein Conformation beta-StrandSequence AlignmentLipoproteinBacterial Outer Membrane ProteinsProteinsREFERENCES
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BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin Α3Β1

2013

ABSTRACT Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal …

Models MolecularProtein familyMolecular Sequence DataIntegrinBiologyModels BiologicalMicrobiologyBiotecnologiaMicrobiologyAmino Acid SequenceBorrelia burgdorferiAdhesins BacterialMolecular BiologyIntegrin alpha3beta1Borrelia Burgdorferi InfectionProteïnes de membranaIntegrin alpha3beta1Articlesbiology.organism_classificationCell biologyBacterial adhesinBorrelia burgdorferibiology.proteinMSCRAMMBacterial outer membraneSequence AlignmentBacterial Outer Membrane ProteinsProtein Binding
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Tick-borne encephalitis virus, Borrelia burgdorferi sensu lato, Borrelia miyamotoi, Anaplasma phagocytophilum and Candidatus Neoehrlichia mikurensis …

2018

The aim of this study was to determine the occurrence of tick-borne pathogens of medical importance in questing ticks collected from five recreationally used islands along the Norwegian coastline. Furthermore, since coinfection may affect the disease severity, this study aimed to determine the extent of coinfection in individual ticks or co-localization of tick-borne pathogens. In all, 4158 questing Ixodes ricinus ticks were analyzed. For detection of tick-borne encephalitis virus (TBEV), nymphs (3690) were analyzed in pools of ten. To detect Borrelia burgdorferi sensu lato, B. miyamotoi, Anaplasma phagocytophilum and Candidatus Neoehrlichia mikurensis, 468 nymphs were analyzed individually…

Nymph0301 basic medicineIxodes ricinus030231 tropical medicine030106 microbiologySheep DiseasesBorrelia miyamotoiReal-Time Polymerase Chain ReactionMicrobiologyEncephalitis Viruses Tick-Borne03 medical and health sciences0302 clinical medicineBorrelia burgdorferi Groupparasitic diseasesPrevalencemedicineAnimalsHumansBorrelia burgdorferiNymphIslandsLyme DiseaseSheepIxodesbiologyCoinfectionNorwayBorreliaEhrlichiosisSequence Analysis DNAbacterial infections and mycosesbiology.organism_classificationmedicine.diseaseVirologyAnaplasma phagocytophilumTick-borne encephalitis virusInfectious DiseasesInsect ScienceCandidatusCoinfectionRecreationbacteriaParasitologyEncephalitis Tick-BorneAnaplasma phagocytophilumTicks and Tick-borne Diseases
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Prevalence of tick-borne pathogens in ticks collected from migratory birds in Latvia.

2014

Migratory birds act as hosts and long-distance vectors for several tick-borne infectious agents. Here, feeding Ixodes ticks were collected from migratory birds during the autumn migration period in Latvia and screened for the presence of epidemiologically important non-viral pathogens. A total of 93 DNA samples of ticks (37 larvae and 56 nymphs) removed from 41 birds (order Passeriformes, 9 species) was tested for Lyme borreliosis spirochaetes, Anaplasma phagocytophilum, Rickettsia spp., and Babesia spp. Borrelia burgdorferi DNA was detected in 18% of the tick samples, and a majority of infected ticks were from thrush (Turdus spp.) birds. Among the infected ticks, Borrelia valaisiana was de…

NymphBorrelia valaisianaanimal diseasesMolecular Sequence DataZoologyBabesiaTickmedicine.disease_causeMicrobiologyMicrobiologyBorreliaparasitic diseasesmedicinePrevalenceAnimalsPasseriformesRickettsiaPhylogenybiologyBase SequenceIxodesBorreliaSequence Analysis DNAbacterial infections and mycosesbiology.organism_classificationAnaplasma phagocytophilumLatviaInfectious DiseasesRickettsiaTick-Borne DiseasesInsect ScienceLarvaBabesiaParasitologyBorrelia gariniiIxodesArachnid VectorsAnaplasma phagocytophilumTicks and tick-borne diseases
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Klinische Manifestation der Lyme-Borreliose im Kindesalter

1989

We report on 4 children with different clinical manifestations of Lyme-Borreliosis. One patient presented with a stage 2 typical aseptic meningitis and 2 others with symptoms of Schonlein-Henoch purpura and rheumatic disease respectively. A further case had bilateral palsy of abducens nerve and unilateral palsy of trochlearis nerve which are described for the first time in Lyme-Borreliosis. Diagnosis was established by detection of specific antibodies to Borrelia in all patients. Differential diagnosis of these symptoms should include Lyme-Borreliosis.

Pediatricsmedicine.medical_specialtyPalsybiologybusiness.industryAseptic meningitisbacterial infections and mycosesmedicine.diseasebiology.organism_classificationPurpuraLyme diseaseBorreliaPediatrics Perinatology and Child HealthMedicineDifferential diagnosisStage (cooking)medicine.symptombusinessAbducens nerveKlinische Pädiatrie
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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.

2019

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore…

Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPaseFEBS lettersReferences
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