0000000000116768

AUTHOR

Jef K. De Brabander

showing 2 related works from this author

Inhibition by cellular vacuolar ATPase impairs human papillomavirus uncoating and infection.

2014

ABSTRACT Several viruses, including human papillomaviruses, depend on endosomal acidification for successful infection. Hence, the multisubunit enzyme vacuolar ATPase (V-ATPase), which is mainly responsible for endosome acidification in the cell, represents an attractive target for antiviral strategies. In the present study, we show that V-ATPase is required for human papillomavirus (HPV) infection and that uncoating/disassembly but not endocytosis is affected by V-ATPase inhibition. The infection inhibitory potencies of saliphenylhalamide, a proven V-ATPase inhibitor, and its derivatives, as well as those of other V-ATPase inhibitors, were analyzed on different HPV types in relevant cell l…

Vacuolar Proton-Translocating ATPasesEndosomeCell SurvivalCellBiologyAlphapapillomavirusEndocytosisInhibitory postsynaptic potentialAntiviral AgentsCell LineViral ProteinsmedicineHumansPharmacology (medical)Vacuolar ATPasePharmacologychemistry.chemical_classificationVacuolar Proton-Translocating ATPasesVirologyEndocytosisCell biologyInfectious Diseasesmedicine.anatomical_structureEnzymechemistryCell cultureHeLa CellsAntimicrobial agents and chemotherapy
researchProduct

Regulation of kynurenine biosynthesis during influenza virus infection.

2017

Influenza A viruses (IAVs) remain serious threats to public health because of the shortage of effective means of control. Developing more effective virus control modalities requires better understanding of virus–host interactions. It has previously been shown that IAV induces the production of kynurenine, which suppresses T-cell responses, enhances pain hypersensitivity and disturbs behaviour in infected animals. However, the regulation of kynurenine biosynthesis during IAV infection remains elusive. Here we showed that IAV infection induced expression of interferons (IFNs), which upregulated production of indoleamine-2,3-dioxygenase (IDO1), which catalysed the kynurenine biosynthesis. Furt…

0301 basic medicineIndoleshost-pathogen interactionViral Nonstructural Proteinsmedicine.disease_causeVirus ReplicationBiochemistryinfluenza viruschemistry.chemical_compoundMiceInfluenza A Virus H1N1 SubtypeInterferonOximesinnate immunityLungOxazolesKynurenineRegulation of gene expressionMice Inbred BALB CSulfonamidesTryptophaninterferon3. Good healthHost-Pathogen InteractionsFemaleMetabolic Networks and Pathwaysmedicine.drugHost–pathogen interaction030106 microbiologyPrimary Cell CultureBiologyta3111Antiviral AgentsVirus03 medical and health sciences3-dioxygenase (IDO1)Orthomyxoviridae InfectionsmedicineAnimalsHumansImmunologic FactorsIndoleamine-Pyrrole 23-DioxygenasePyrrolesMolecular BiologyInnate immune systemta1184Macrophagesta1183ta1182Cell BiologyVirologyindoleamine-pyrrole 2Thiazoles030104 developmental biologyHerpes simplex virusViral replicationchemistryGene Expression RegulationInterferonsTranscriptomeKynurenineThe FEBS journal
researchProduct