Search results for "Viruses"

showing 10 items of 1182 documents

Possible Transmission Flow of SARS-CoV-2 Based on ACE2 Features

2020

Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) that is engendering the severe coronavirus disease 2019 (COVID-19) pandemic. The spike (S) protein receptor-binding domain (RBD) of SARS-CoV-2 binds to the three sub-domains viz. amino acids (aa) 22&ndash

Pan troglodytesvirusesProtein domainACE2Pharmaceutical ScienceBiologyArticleAnalytical Chemistrylcsh:QD241-44103 medical and health sciencesDogs0302 clinical medicineProtein DomainsSpecies Specificitylcsh:Organic chemistryDrug DiscoveryAnimalsHumansviral spike receptor-binding domainPhysical and Theoretical ChemistryReceptor030304 developmental biologychemistry.chemical_classification0303 health sciencesCATSSARS-CoV-2Transmission (medicine)fungiOrganic ChemistrytransmissionCOVID-19virus diseasesbioinformaticsMetabolismVirologyAmino acidEnzymechemistryChemistry (miscellaneous)030220 oncology & carcinogenesisSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2CatsMolecular MedicineCattleAngiotensin-Converting Enzyme 2hormones hormone substitutes and hormone antagonistsMolecules
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Diversity and Evolution of papillomaviruses

2017

1.1. Introducción Con el fin de averiguar las causas de las devastadoras epidemias de finales del siglo XIX, se llevaron a cabo diferentes estudios que dieron como resultado la identificación de unos nuevos agentes infecciosos, para los que se acuñó el nombre de “virus”. Desde entonces el descubrimiento de nuevos virus ha sido incesante, lo que llevó, en los años 70, a la creación de un organismo encargado de desarrollar, refinar y mantener la clasificación taxonómica de los virus, el Comité Internacional de Taxonomía Viral (ICTV), en el seno de la Unión Internacional de Sociedades Microbiológicas (IUMS). En 2014 este organismo había reconocido 3.186 especies virales pertenecientes a 104 fa…

Papillomavirus diversityViral diversityCo-evolutionIncongruent gene treesPapillomavirus classification310911 Ciencias Veterinarias virología2499 Evolución y Diversidad242091 Virología AnimalDNA virusesInfectionAnimal virusesPhylogenetic inferenceCancer
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Prevalence of human parvovirus B19 in blood donors as determined by a haemagglutination assay and verified by the polymerase chain reaction

2002

Background and Objectives Transmission of human parvovirus B19 (PV B19) by transfusion of blood and blood products is well documented. Although PV B19 infection is connected with severe complications in some recipients, donor screening is not yet mandatory. In this study the prevalence of PV B19, as detected by a haemagglutination assay (the Human PV B19 Antigen-Test), was assessed. In addition, the persistence of B19 DNA and the serological status of blood donors was also assessed. The specificity and utility of the Human PV B19 Antigen-Test for donor screening was investigated and compared with other screening strategies. Materials and Methods The prevalence of PV B19 viraemia was assesse…

ParvoviridaeHemagglutination assaybiologyHemagglutinationvirusesvirus diseasesViremiaHematologyGeneral Medicinebiology.organism_classificationmedicine.diseaseVirologylaw.inventionSerologylawhemic and lymphatic diseasesImmunologybiology.proteinmedicineViral diseaseNeutralizing antibodyPolymerase chain reactionVox Sanguinis
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Distribution and dynamics of transcription-associated proteins during parvovirus infection.

2012

Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins. peerReviewed

Parvovirus transkriptioproteiinitvirusesdynamiikka
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Role of Recycling Endosomes and Lysosomes in Dynein-Dependent Entry of Canine Parvovirus

2002

ABSTRACT Canine parvovirus (CPV) is a nonenveloped virus with a 5-kb single-stranded DNA genome. Lysosomotropic agents and low temperature are known to prevent CPV infection, indicating that the virus enters its host cells by endocytosis and requires an acidic intracellular compartment for penetration into the cytoplasm. After escape from the endocytotic vesicles, CPV is transported to the nucleus for replication. In the present study the intracellular entry pathway of the canine parvovirus in NLFK (Nordisk Laboratory feline kidney) cells was studied. After clustering in clathrin-coated pits and being taken up in coated vesicles, CPV colocalized with coendocytosed transferrin in endosomes r…

Parvovirus CanineEndosomeanimal diseasesvirusesImmunologyDyneinCoated vesicleEndosomesBiologyEndocytosisMicrobiologyMicrotubulesCell LineDogsMicrotubuleVirologyAnimalsMicroscopy ImmunoelectronIn Situ Hybridization FluorescenceMicroscopy ConfocalVesicleEndoplasmic reticulumDyneinsEndocytosisCell biologyVirus-Cell InteractionsCytoplasmInsect ScienceLysosomes
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Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Parvovirus CanineRecombinant Fusion Proteinsanimal diseasesvirusesGreen Fluorescent ProteinsBiophysicsMammalian expressionBiochemistryCell LineGreen fluorescent proteinTransduction (genetics)DogsTransduction GeneticStructural BiologyGeneticsAnimalsBaculovirusCanine parvovirusMolecular BiologyCell NucleusEnhanced green fluorescent proteinbiologyParvovirusCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyCell biologyCapsidCytoplasmCell cultureCatsCapsid ProteinsBaculoviridaeNuclear localization sequenceFEBS Letters
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Assembly of fluorescent chimeric virus-like particles of canine parvovirus in insect cells

2004

Canine parvovirus (CPV) is a small non-enveloped ssDNA virus composed of the viral proteins VP1, VP2, and VP3 with a T=1 icosahedral symmetry. VP2 is nested in VP1 and the two proteins are produced by differential splicing of a primary transcript of the right ORF of the viral genome. The VP2 protein can be further proteolytically cleaved to form VP3. Previous studies have shown that VP1 and VP3 are unnecessary for capsid formation and consequently, that VP2 alone is sufficient for assembly. We have hypothesized that insertion of the enhanced green fluorescent protein (EGFP) at the N-terminus of VP2 could be carried out without altering assembly. To investigate the possibility to develop flu…

Parvovirus CanineRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsHeterologousFluorescence correlation spectroscopySpodopteraBiochemistryVirusCell LineInclusion Bodies ViralGreen fluorescent proteinAnimalsAmino Acid SequenceMolecular BiologyMicroscopy ConfocalBase SequencebiologyChimeraVirus AssemblyCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFusion proteinLuminescent ProteinsMicroscopy ElectronCapsidRNA splicingCapsid ProteinsPlasmidsBiochemical and Biophysical Research Communications
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Distribution and Dynamics of Transcription-Associated Proteins during Parvovirus Infection

2012

ABSTRACT Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins.

Parvovirus CanineViral nonstructural proteinvirusesImmunologyMicrobiologyParvoviridae Infections03 medical and health sciencesVirologyAnimalsTranscription factor030304 developmental biology0303 health sciencesbiologyParvovirusBinding protein030302 biochemistry & molecular biologyCanine parvovirusFluorescence recovery after photobleachingbiology.organism_classificationMolecular biology3. Good healthVirus-Cell InteractionsCell CompartmentationInsect Sciencebiology.proteinTATA-binding proteinTranscription factor II BSubcellular FractionsTranscription Factors
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Detection of canine parvovirus antigens with antibodies to synthetic peptides

1996

Antibodies produced in rabbits against an 18-amino acid peptide (peptide 1, NSLPQSEGATNFGDIGVP) of capsid protein VP2/residues 292-309 of canine parvovirus (CPV) or against an 18-amino acid peptide (peptide 2, GKRNTVLFHGPASTKGKS) of nonstructural protein NS1/residues 391-409 of CPV identified, in immunofluorescence analysis, viral antigens in canine A 72 cells infected with CPV. Antibodies to peptide 2 also identified viral antigens in bovine cells infected with bovine parvovirus. In western blot analysis, antibodies to peptide 1 and peptide 2 also detected viral antigens derived from blue fox parvovirus, feline parvovirus, mink enteritis virus and raccoon dog parvovirus. The peptide antibo…

Parvovirus Canineanimal diseasesvirusesBlotting WesternMolecular Sequence DataFoxesEnzyme-Linked Immunosorbent AssayAntibodies ViralVirusParvovirusCapsidDogsAntigenVirologyAnimalsAmino Acid SequenceFluorescent Antibody Technique IndirectAntigens ViralPeptide sequenceParvoviridaebiologyParvovirusCanine parvovirusvirus diseasesGeneral MedicineBovine parvovirusbiology.organism_classificationVirologyMink enteritis virusMinkCatsCapsid ProteinsCattleRaccoonsRabbitsFeline Panleukopenia VirusArchives of Virology
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Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection

2015

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Parvovirus Canineanimal diseasesvirusesnuclear pore complexesImmunologyMicrobiologyParvoviridae InfectionsCapsidDogsVirologymedicineotorhinolaryngologic diseasesAnimalsDog DiseasesNuclear poreparvovovirusCell NucleusNuclear LaminaLamin Type BbiologyParvovirusParvovirus infectionCanine parvovirusLamin Type Abiology.organism_classificationmedicine.diseaseVirologyVirus-Cell InteractionsCell biologyNuclear Pore Complex ProteinsCell nucleusstomatognathic diseasesmedicine.anatomical_structureInsect ScienceNuclear PoreNuclear laminaNucleusLamin
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