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dc.contributor.author Vörös Zsuzsanna
dc.contributor.author Csik Gabriella
dc.contributor.author Herényi Levente
dc.contributor.author Kellermayer Miklós
dc.date.accessioned 2018-10-15T06:39:56Z
dc.date.available 2018-10-15T06:39:56Z
dc.date.issued 2018
dc.identifier.citation pagination=e01236-18.; journalVolume=92; journalIssue=20; journalTitle=JOURNAL OF VIROLOGY;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/6452
dc.identifier.uri doi:10.1128/JVI.01236-18
dc.description.abstract Viruses are nanoscale infectious agents, which may be inactivated by heat treatment. The global molecular mechanisms of virus inactivation and the thermally-induced structural changes in viruses are not fully understood. Here we measured the heat-induced changes in the properties of T7 bacteriophage particles exposed to two-stage (65 degrees C and 80 degrees C) thermal effect, by using AFM-based nanomechanical and topographical measurements. We found that exposure to 65 degrees C led to the release of genomic DNA and to the loss of the capsid tail, hence the T7 particles became destabilized. Further heating to 80 degrees C surprisingly led to an increase in mechanical stability, due likely to partial denaturation of the capsomeric proteins kept within the global capsid arrangement.IMPORTANCE Even though the loss of DNA, caused by heat treatment, destabilizes the T7 phage, its capsid is remarkably able to withstand high temperatures with a more-or-less intact global topographical structure. Thus, partial denaturation within the global structural constraints of the viral capsid may have a stabilizing effect. Understanding the structural design of viruses may help in constructing artificial nanocapsules for the packaging and delivery of materials under harsh environmental conditions.
dc.relation.ispartof urn:issn:0022-538X
dc.title Temperature-dependent nanomechanics and topography of bacteriophage T7.
dc.type Journal Article
dc.date.updated 2018-09-14T09:14:39Z
dc.language.rfc3066 en
dc.identifier.mtmt 3405413
dc.identifier.pubmed 30089696
dc.contributor.department SE/AOK/I/Biofizikai és Sugárbiológiai Intézet
dc.contributor.institution Semmelweis Egyetem
dc.mtmt.swordnote FELTÖLTŐ: Haluszka Dóra - haluszka.dora@med.semmelweis-univ.hu # Kötet ismeretlen


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