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dc.contributor.author
Mouna, Lina
dc.contributor.author
Hernandez, Eva
dc.contributor.author
Bonte, Dorine
dc.contributor.author
Brost, Rebekka
dc.contributor.author
Amazit, Larbi
dc.contributor.author
Delgui, Laura Ruth
dc.contributor.author
Brune, Wolfram
dc.contributor.author
Geballe, Adam P.
dc.contributor.author
Beau, Isabelle
dc.contributor.author
Esclatine, Audrey
dc.date.available
2018-04-10T12:52:06Z
dc.date.issued
2015-12
dc.identifier.citation
Mouna, Lina; Hernandez, Eva; Bonte, Dorine; Brost, Rebekka; Amazit, Larbi; et al.; Analysis of the role of autophagy inhibition by two complementary human cytomegalovirus BECN1/Beclin 1-binding proteins; Landes Bioscience; Autophagy; 12; 2; 12-2015; 327-342
dc.identifier.issn
1554-8627
dc.identifier.uri
http://hdl.handle.net/11336/41469
dc.description.abstract
Autophagy is activated early after human cytomegalovirus (HCMV) infection, but lateron the virus blocks autophagy. Here we characterized 2 HCMV proteins, TRS1 andIRS1, which inhibit autophagy during infection. Expression of either TRS1 or IRS1 wasable to block autophagy in different cell lines, independently of the EIF2S1 kinase,EIF2AK2/PKR. Instead, TRS1 and IRS1 interacted with the autophagy proteinBECN1/Beclin 1. We mapped the BECN1-binding domain (BBD) of IRS1 and TRS1 andfound it to be essential for autophagy inhibition. Mutant viruses that express only IRS1or TRS1 partially controlled autophagy, whereas a double mutant virus expressingneither protein stimulated autophagy. A mutant virus that did not express IRS1 andexpressed a truncated form of TRS1 in which the BBD was deleted, failed to controlautophagy. However, this mutant virus had similar replication kinetics as wild-type virus,suggesting that autophagy inhibition is not critical for viral replication. In fact, usingpharmacological modulators of autophagy and inhibition of autophagy by shRNAknockdown, we discovered that stimulating autophagy enhanced viral replication.Conversely, inhibiting autophagy decreased HCMV infection. Thus, our resultsdemonstrate a new proviral role of autophagy for a DNA virus
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Landes Bioscience
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Autophagy
dc.subject
Becn1
dc.subject
Cytomegalovirus
dc.subject
Eif2ak2/Pkr
dc.subject
Irs1
dc.subject
Trs1
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Analysis of the role of autophagy inhibition by two complementary human cytomegalovirus BECN1/Beclin 1-binding proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-27T13:36:59Z
dc.journal.volume
12
dc.journal.number
2
dc.journal.pagination
327-342
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Austin, Texas
dc.description.fil
Fil: Mouna, Lina. Université Paris Sud; Francia
dc.description.fil
Fil: Hernandez, Eva. Université Paris Sud; Francia
dc.description.fil
Fil: Bonte, Dorine. Centre National de la Recherche Scientifique; Francia
dc.description.fil
Fil: Brost, Rebekka. Heinrich Pette Institute; Alemania
dc.description.fil
Fil: Amazit, Larbi. Université Paris Sud; Francia
dc.description.fil
Fil: Delgui, Laura Ruth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
dc.description.fil
Fil: Brune, Wolfram. Heinrich Pette Institute; Alemania
dc.description.fil
Fil: Geballe, Adam P.. University of Washington; Estados Unidos
dc.description.fil
Fil: Beau, Isabelle. Université Paris Sud; Francia
dc.description.fil
Fil: Esclatine, Audrey. Université Paris Sud; Francia
dc.journal.title
Autophagy
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1080/15548627.2015.1125071
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/15548627.2015.1125071
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