The Experts below are selected from a list of 243165 Experts worldwide ranked by ideXlab platform
Cathy L. Miller - One of the best experts on this subject based on the ideXlab platform.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
bioRxiv, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α which promotes formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early, then interferes with SG formation as infection proceeds. In this work, we found that SG associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of SG effector Protein, G3BP1, with MRV non-structural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that the association and VF Localization of G3BP1 is not occurring solely through RNA or ribosomal binding, but requires both RNA and ribosomal binding domains of G3BP1 for maximal VFL Localization and σNS association. Co-expression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with and reLocalization of G3BP1 to the VF periphery plays a role in SG disruption to facilitate MRV replication in the host translational shutoff environment.
Theodorus W J Gadella - One of the best experts on this subject based on the ideXlab platform.
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bright monomeric red fluorescent Protein with an extended fluorescence lifetime
Nature Methods, 2007Co-Authors: Ekaterina M. Merzlyak, Sergey Lukyanov, Dmitry Shcherbo, Arkady F. Fradkov, Konstantin A. Lukyanov, Joachim Goedhart, Mariya E Bulina, Aleksandr S Shcheglov, Anna Gaintzeva, Theodorus W J GadellaAbstract:Fluorescent Proteins have become extremely popular tools for in vivo imaging and especially for the study of Localization, motility and interaction of Proteins in living cells. Here we report TagRFP, a monomeric red fluorescent Protein, which is characterized by high brightness, complete chromophore maturation, prolonged fluorescence lifetime and high pH-stability. These properties make TagRFP an excellent tag for Protein Localization studies and fluorescence resonance energy transfer (FRET) applications.
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bright monomeric red fluorescent Protein with an extended fluorescence lifetime
Nature Methods, 2007Co-Authors: Ekaterina M. Merzlyak, Sergey Lukyanov, Dmitry Shcherbo, Arkady F. Fradkov, Konstantin A. Lukyanov, Joachim Goedhart, Mariya E Bulina, Aleksandr S Shcheglov, Anna Gaintzeva, Theodorus W J GadellaAbstract:Fluorescent Proteins have become extremely popular tools for in vivo imaging and especially for the study of Localization, motility and interaction of Proteins in living cells. Here we report TagRFP, a monomeric red fluorescent Protein, which is characterized by high brightness, complete chromophore maturation, prolonged fluorescence lifetime and high pH-stability. These properties make TagRFP an excellent tag for Protein Localization studies and fluorescence resonance energy transfer (FRET) applications.
Promisree Choudhury - One of the best experts on this subject based on the ideXlab platform.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
bioRxiv, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α which promotes formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early, then interferes with SG formation as infection proceeds. In this work, we found that SG associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of SG effector Protein, G3BP1, with MRV non-structural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that the association and VF Localization of G3BP1 is not occurring solely through RNA or ribosomal binding, but requires both RNA and ribosomal binding domains of G3BP1 for maximal VFL Localization and σNS association. Co-expression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with and reLocalization of G3BP1 to the VF periphery plays a role in SG disruption to facilitate MRV replication in the host translational shutoff environment.
Ekaterina M. Merzlyak - One of the best experts on this subject based on the ideXlab platform.
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bright monomeric red fluorescent Protein with an extended fluorescence lifetime
Nature Methods, 2007Co-Authors: Ekaterina M. Merzlyak, Sergey Lukyanov, Dmitry Shcherbo, Arkady F. Fradkov, Konstantin A. Lukyanov, Joachim Goedhart, Mariya E Bulina, Aleksandr S Shcheglov, Anna Gaintzeva, Theodorus W J GadellaAbstract:Fluorescent Proteins have become extremely popular tools for in vivo imaging and especially for the study of Localization, motility and interaction of Proteins in living cells. Here we report TagRFP, a monomeric red fluorescent Protein, which is characterized by high brightness, complete chromophore maturation, prolonged fluorescence lifetime and high pH-stability. These properties make TagRFP an excellent tag for Protein Localization studies and fluorescence resonance energy transfer (FRET) applications.
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bright monomeric red fluorescent Protein with an extended fluorescence lifetime
Nature Methods, 2007Co-Authors: Ekaterina M. Merzlyak, Sergey Lukyanov, Dmitry Shcherbo, Arkady F. Fradkov, Konstantin A. Lukyanov, Joachim Goedhart, Mariya E Bulina, Aleksandr S Shcheglov, Anna Gaintzeva, Theodorus W J GadellaAbstract:Fluorescent Proteins have become extremely popular tools for in vivo imaging and especially for the study of Localization, motility and interaction of Proteins in living cells. Here we report TagRFP, a monomeric red fluorescent Protein, which is characterized by high brightness, complete chromophore maturation, prolonged fluorescence lifetime and high pH-stability. These properties make TagRFP an excellent tag for Protein Localization studies and fluorescence resonance energy transfer (FRET) applications.
Luke D Bussiere - One of the best experts on this subject based on the ideXlab platform.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
Journal of Virology, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:ABSTRACT Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α, which promotes the formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early and then interferes with SG formation as infection proceeds. In this work, we found that SG-associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of the SG effector Protein, Ras-GAP SH3-binding Protein 1 (G3BP1), with the MRV nonstructural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that σNS association and VF Localization phenotypes of G3BP1 do not occur solely through RNA or ribosomal binding but require both the RRM and RGG domains of G3BP1 for maximal viral-factory-like structure (VFL) Localization and σNS association. Coexpression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with G3BP1 and reLocalization of G3BP1 to the VF periphery play roles in SG disruption to facilitate MRV replication in the host translational shutoff environment. IMPORTANCE SGs and SG effector Proteins have emerged as important, yet poorly understood, players in the host9s innate immune response to virus infection. MRV infection induces SGs early during infection that are dispersed and/or prevented from forming during late stages of infection despite continued activation of the eIF2α signaling pathway. Cellular and viral components involved in disruption of SGs during late stages of MRV infection remain to be elucidated. This work provides evidence that MRV disruption of SGs may be facilitated by association of the MRV nonstructural Protein σNS with the major SG effector Protein G3BP1 and subsequent Localization of G3BP1 and other SG-associated Proteins around the peripheries of virus-encoded factories, interrupting the normal formation of SGs. Our findings also reveal the importance of G3BP1 as an inhibitor of MRV replication during infection for the first time.
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mammalian orthoreovirus factories modulate stress granule Protein Localization by interaction with g3bp1
bioRxiv, 2017Co-Authors: Promisree Choudhury, Luke D Bussiere, Cathy L. MillerAbstract:Mammalian orthoreovirus (MRV) infection induces phosphorylation of translation initiation factor eIF2α which promotes formation of discrete cytoplasmic inclusions, termed stress granules (SGs). SGs are emerging as a component of the innate immune response to virus infection, and modulation of SG assembly is a common mechanism employed by viruses to counter this antiviral response. We previously showed that MRV infection induces SGs early, then interferes with SG formation as infection proceeds. In this work, we found that SG associated Proteins localized to the periphery of virus-encoded cytoplasmic structures, termed virus factories (VFs), where viral transcription, translation, and replication occur. The Localization of SG Proteins to VFs was dependent on polysome dissociation and occurred via association of SG effector Protein, G3BP1, with MRV non-structural Protein σNS, which localizes to VFs via association with VF nucleating Protein, μNS. Deletion analysis of the σNS RNA binding domain and G3BP1 RNA (RRM) and ribosomal (RGG) binding domains showed that the association and VF Localization of G3BP1 is not occurring solely through RNA or ribosomal binding, but requires both RNA and ribosomal binding domains of G3BP1 for maximal VFL Localization and σNS association. Co-expression of σNS and μNS resulted in disruption of normal SG puncta, and in cells lacking G3BP1, MRV replication was enhanced in a manner correlating with strain-dependent induction of host translation shutoff. These results suggest that σNS association with and reLocalization of G3BP1 to the VF periphery plays a role in SG disruption to facilitate MRV replication in the host translational shutoff environment.
