dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorStauffer, Fausto
dc.creatorDe Miranda, Joari
dc.creatorSchechter, Marcos C.
dc.creatorCarneiro, Fabiana A.
dc.creatorSalgado, Leonardo T.
dc.creatorMachado, Gisele Fabrino
dc.creatorDa Poian, Andrea T.
dc.date2014-05-27T11:22:21Z
dc.date2016-10-25T18:23:24Z
dc.date2014-05-27T11:22:21Z
dc.date2016-10-25T18:23:24Z
dc.date2007-01-01
dc.date.accessioned2017-04-06T01:23:10Z
dc.date.available2017-04-06T01:23:10Z
dc.identifierAntiviral Research, v. 73, n. 1, p. 31-39, 2007.
dc.identifier0166-3542
dc.identifierhttp://hdl.handle.net/11449/69438
dc.identifierhttp://acervodigital.unesp.br/handle/11449/69438
dc.identifier10.1016/j.antiviral.2006.07.007
dc.identifierWOS:000244020200004
dc.identifier2-s2.0-33846136390
dc.identifierhttp://dx.doi.org/10.1016/j.antiviral.2006.07.007
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/890688
dc.descriptionMembrane fusion is an essential step in the entry of enveloped viruses into their host cells triggered by conformational changes in viral glycoproteins. We have demonstrated previously that modification of vesicular stomatitis virus (VSV) with diethylpyrocarbonate (DEPC) abolished conformational changes on VSV glycoprotein and the fusion reaction catalyzed by the virus. In the present study, we evaluated whether treatment with DEPC was able to inactivate the virus. Infectivity and viral replication were abolished by viral treatment with 0.5 mM DEPC. Mortality profile and inflammatory response in the central nervous system indicated that G protein modification with DEPC eliminates the ability of the virus to cause disease. In addition, DEPC treatment did not alter the conformational integrity of surface proteins of inactivated VSV as demonstrated by transmission electron microscopy and competitive ELISA. Taken together, our results suggest a potential use of histidine (His) modification to the development of a new process of viral inactivation based on fusion inhibition. © 2006 Elsevier B.V. All rights reserved.
dc.languageeng
dc.relationAntiviral Research
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectDiethylpyrocarbonate
dc.subjectMembrane fusion
dc.subjectVesicular stomatitis virus
dc.subjectViral inactivation
dc.subjectdiethyl pyrocarbonate
dc.subjecthistidine
dc.subjecthydroxylamine
dc.subjectvirus glycoprotein
dc.subjectanimal cell
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectanimal tissue
dc.subjectbrain infection
dc.subjectchemical modification
dc.subjectconformational transition
dc.subjectcontrolled study
dc.subjectdrug dose comparison
dc.subjectenzyme linked immunosorbent assay
dc.subjectmale
dc.subjectmembrane fusion
dc.subjectmouse
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein conformation
dc.subjectRNA virus infection
dc.subjecttransmission electron microscopy
dc.subjectvirus cell interaction
dc.subjectvirus inactivation
dc.subjectvirus infectivity
dc.subjectvirus replication
dc.subjectvirus titration
dc.subjectAnimals
dc.subjectCricetinae
dc.subjectDiethyl Pyrocarbonate
dc.subjectDisease Models, Animal
dc.subjectHumans
dc.subjectMembrane Fusion
dc.subjectMembrane Glycoproteins
dc.subjectMice
dc.subjectMice, Inbred BALB C
dc.subjectVesicular stomatitis-Indiana virus
dc.subjectViral Envelope Proteins
dc.subjectVirus Inactivation
dc.titleInactivation of vesicular stomatitis virus through inhibition of membrane fusion by chemical modification of the viral glycoprotein
dc.typeOtro


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