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Article: A novel inhibitory mechanism of mitochondrion-dependent apoptosis by a herpesviral protein

TitleA novel inhibitory mechanism of mitochondrion-dependent apoptosis by a herpesviral protein
Authors
Issue Date2007
Citation
PLoS Pathogens, 2007, v. 3, n. 12, p. 1849-1865 How to Cite?
AbstractUpon viral infection, cells undergo apoptosis as a defense against viral replication. Viruses, in turn, have evolved elaborate mechanisms to subvert apoptotic processes. Here, we report that a novel viral mitochondrial anti-apoptotic protein (vMAP) of murine γ-herpesvirus 68 (γHV-68) interacts with Bcl-2 and voltage-dependent anion channel 1 (VDAC1) in a genetically separable manner. The N-terminal region of vMAP interacted with Bcl-2, and this interaction markedly increased not only Bcl-2 recruitment to mitochondria but also its avidity for BH3-only pro-apoptotic proteins, thereby suppressing Bax mitochondrial translocation and activation. In addition, the central and C-terminal hydrophobic regions of vMAP interacted with VDAC1. Consequently, these interactions resulted in the effective inhibition of cytochrome c release, leading to the comprehensive inhibition of mitochondrion-mediated apoptosis. Finally, vMAP gene was required for efficient γHV-68 lytic replication in normal cells, but not in mitochondrial apoptosis-deficient cells. These results demonstrate that γHV-68 vMAP independently targets two important regulators of mitochondrial apoptosis-mediated intracellular innate immunity, allowing efficient viral lytic replication. © 2007 Feng et al.
Persistent Identifierhttp://hdl.handle.net/10722/285918
ISSN
2019 Impact Factor: 6.218
2015 SCImago Journal Rankings: 5.185
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorFeng, Pinghui-
dc.contributor.authorLiang, Chengyu-
dc.contributor.authorShin, Young C.-
dc.contributor.authorE, Xiaofei-
dc.contributor.authorZhang, Weijun-
dc.contributor.authorGravel, Robyn-
dc.contributor.authorWu, Ting Ting-
dc.contributor.authorSun, Ren-
dc.contributor.authorUsherwood, Edward-
dc.contributor.authorJung, Jae U.-
dc.date.accessioned2020-08-18T04:56:59Z-
dc.date.available2020-08-18T04:56:59Z-
dc.date.issued2007-
dc.identifier.citationPLoS Pathogens, 2007, v. 3, n. 12, p. 1849-1865-
dc.identifier.issn1553-7366-
dc.identifier.urihttp://hdl.handle.net/10722/285918-
dc.description.abstractUpon viral infection, cells undergo apoptosis as a defense against viral replication. Viruses, in turn, have evolved elaborate mechanisms to subvert apoptotic processes. Here, we report that a novel viral mitochondrial anti-apoptotic protein (vMAP) of murine γ-herpesvirus 68 (γHV-68) interacts with Bcl-2 and voltage-dependent anion channel 1 (VDAC1) in a genetically separable manner. The N-terminal region of vMAP interacted with Bcl-2, and this interaction markedly increased not only Bcl-2 recruitment to mitochondria but also its avidity for BH3-only pro-apoptotic proteins, thereby suppressing Bax mitochondrial translocation and activation. In addition, the central and C-terminal hydrophobic regions of vMAP interacted with VDAC1. Consequently, these interactions resulted in the effective inhibition of cytochrome c release, leading to the comprehensive inhibition of mitochondrion-mediated apoptosis. Finally, vMAP gene was required for efficient γHV-68 lytic replication in normal cells, but not in mitochondrial apoptosis-deficient cells. These results demonstrate that γHV-68 vMAP independently targets two important regulators of mitochondrial apoptosis-mediated intracellular innate immunity, allowing efficient viral lytic replication. © 2007 Feng et al.-
dc.languageeng-
dc.relation.ispartofPLoS Pathogens-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleA novel inhibitory mechanism of mitochondrion-dependent apoptosis by a herpesviral protein-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.ppat.0030174-
dc.identifier.pmid18069888-
dc.identifier.pmcidPMC2134948-
dc.identifier.scopuseid_2-s2.0-38049069826-
dc.identifier.volume3-
dc.identifier.issue12-
dc.identifier.spage1849-
dc.identifier.epage1865-
dc.identifier.eissn1553-7374-
dc.identifier.f10001097817-

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