HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells

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dc.contributor.authorSainis, L.en
dc.contributor.authorAngelidis, C.en
dc.contributor.authorPagoulatos, G. N.en
dc.contributor.authorLazaridis, L.en
dc.date.accessioned2015-11-24T19:13:02Z
dc.date.available2015-11-24T19:13:02Z
dc.identifier.issn1355-8145-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21147
dc.rightsDefault Licence-
dc.subject3T3 Cellsen
dc.subjectAnimalsen
dc.subjectAntigens, Polyomavirus Transforming/*metabolismen
dc.subjectCOS Cellsen
dc.subjectCapsid/metabolismen
dc.subject*Capsid Proteinsen
dc.subjectCarrier Proteins/*metabolismen
dc.subjectFluorescent Antibody Techniqueen
dc.subjectHSC70 Heat-Shock Proteinsen
dc.subject*HSP70 Heat-Shock Proteinsen
dc.subjectHaplorhinien
dc.subjectInterferon-gamma/pharmacologyen
dc.subjectIntracellular Fluid/metabolismen
dc.subjectMiceen
dc.subjectPrecipitin Testsen
dc.subjectProtein Bindingen
dc.subjectSimian virus 40/metabolism/*physiologyen
dc.titleHSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cellsen
heal.abstractSV40 belongs to a group of DNA tumor viruses which induce the expression of the 70 Kd heat shock proteins, but the meaning of this induction remains unclear. Investigating the role of hsc70 in the SV40 life cycle, we found that the protein translocates to the nucleus late in infection of permissive CV1 cells, in contrast to infected nonpermissive BALB/3T3 and NIH/3T3 cells in which hsc70 remains cytoplasmic. Moreover, the pattern of hsc70 nuclear staining was diffused and clearly distinguishable from that observed after heat shock. In addition hsc70 late in infection coimmunoprecipitated with the viral capsid protein VP1, suggesting a role in the process of viral packaging. Interactions of hsc70 with the early viral oncoprotein T antigen were observed only in nonpermissive cells, indicating that the binding of the above proteins is specific to cells that do not support viral propagation. Finally, treatment of permissive CV1 cells with interferon gamma, a known antiviral cytokine, resulted in hsc70 binding to T antigen. Our results suggest that the role of hsc70 in the process of SV40 infection is directly related to the ability of the host cells to support viral propagation and is clearly different between permissive and nonpermissive cell lines.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11147964-
heal.journalNameCell Stress Chaperonesen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate2000-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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