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  1. Article ; Online: Rho'ing in and out of cells: viral interactions with Rho GTPase signaling.

    Van den Broeke, Céline / Jacob, Thary / Favoreel, Herman W

    Small GTPases

    2014  Volume 5, Page(s) e28318

    Abstract: Rho GTPases are key regulators of actin and microtubule dynamics and organization. Increasing evidence shows that many viruses have evolved diverse interactions with Rho GTPase signaling and manipulate them for their own benefit. In this review, we ... ...

    Abstract Rho GTPases are key regulators of actin and microtubule dynamics and organization. Increasing evidence shows that many viruses have evolved diverse interactions with Rho GTPase signaling and manipulate them for their own benefit. In this review, we discuss how Rho GTPase signaling interferes with many steps in the viral replication cycle, especially entry, replication, and spread. Seen the diversity between viruses, it is not surprising that there is considerable variability in viral interactions with Rho GTPase signaling. However, several largely common effects on Rho GTPases and actin architecture and microtubule dynamics have been reported. For some of these processes, the molecular signaling and biological consequences are well documented while for others we just begin to understand them. A better knowledge and identification of common threads in the different viral interactions with Rho GTPase signaling and their ultimate consequences for virus and host may pave the way toward the development of new antiviral drugs that may target different viruses.
    MeSH term(s) Actins/metabolism ; Clathrin/metabolism ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Endocytosis ; Humans ; Microtubules/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; Viruses/metabolism ; Viruses/pathogenicity ; rho GTP-Binding Proteins/metabolism
    Chemical Substances Actins ; Clathrin ; rho GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-03-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2682247-7
    ISSN 2154-1256 ; 2154-1248
    ISSN (online) 2154-1256
    ISSN 2154-1248
    DOI 10.4161/sgtp.28318
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Pseudorabies virus US3 triggers RhoA phosphorylation to reorganize the actin cytoskeleton.

    Jacob, Thary / Broeke, Céline Van den / Waesberghe, Cliff Van / Troys, Leen Van / Favoreel, Herman W

    The Journal of general virology

    2015  Volume 96, Issue 8, Page(s) 2328–2335

    Abstract: The conserved alphaherpesvirus serine/threonine kinase US3 causes dramatic changes in the actin cytoskeleton, consisting of actin stress fibre breakdown and protrusion formation, associated with increased virus spread. Here, we showed that US3 expression ...

    Abstract The conserved alphaherpesvirus serine/threonine kinase US3 causes dramatic changes in the actin cytoskeleton, consisting of actin stress fibre breakdown and protrusion formation, associated with increased virus spread. Here, we showed that US3 expression led to RhoA phosphorylation at serine 188 (S188), one of the hallmarks of suppressed RhoA signalling, and that expression of a non-phosphorylatable RhoA variant interfered with the ability of US3 to induce actin rearrangements. Furthermore, inhibition of cellular protein kinase A (PKA) eliminated the ability of US3 to induce S188 RhoA phosphorylation, pointing to a role for PKA in US3-induced RhoA phosphorylation. Hence, the US3 kinase leads to PKA-dependent S188 RhoA phosphorylation, which contributes to US3-mediated actin rearrangements. Our data suggest that US3 efficiently usurps the antagonistic RhoA and Cdc42/Rac1/p21-activated kinase signalling branches to rearrange the actin cytoskeleton.
    MeSH term(s) Actins/metabolism ; Animals ; Cytoskeleton/metabolism ; Herpesvirus 1, Suid/enzymology ; Herpesvirus 1, Suid/genetics ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Pseudorabies/enzymology ; Pseudorabies/metabolism ; Pseudorabies/virology ; Swine ; Swine Diseases/enzymology ; Swine Diseases/metabolism ; Swine Diseases/virology ; Viral Proteins/genetics ; Viral Proteins/metabolism ; rhoA GTP-Binding Protein/chemistry ; rhoA GTP-Binding Protein/genetics ; rhoA GTP-Binding Protein/metabolism
    Chemical Substances Actins ; Viral Proteins ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
    Language English
    Publishing date 2015-04-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 219316-4
    ISSN 1465-2099 ; 0022-1317
    ISSN (online) 1465-2099
    ISSN 0022-1317
    DOI 10.1099/vir.0.000152
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 610: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Viral serine/threonine protein kinases.

    Jacob, Thary / Van den Broeke, Céline / Favoreel, Herman W

    Journal of virology

    2010  Volume 85, Issue 3, Page(s) 1158–1173

    Abstract: Phosphorylation represents one the most abundant and important posttranslational modifications of proteins, including viral proteins. Virus-encoded serine/threonine protein kinases appear to be a feature that is unique to large DNA viruses. Although the ... ...

    Abstract Phosphorylation represents one the most abundant and important posttranslational modifications of proteins, including viral proteins. Virus-encoded serine/threonine protein kinases appear to be a feature that is unique to large DNA viruses. Although the importance of these kinases for virus replication in cell culture is variable, they invariably play important roles in virus virulence. The current review provides an overview of the different viral serine/threonine protein kinases of several large DNA viruses and discusses their function, importance, and potential as antiviral drug targets.
    MeSH term(s) DNA Viruses/enzymology ; Humans ; Phosphorylation ; Protein Processing, Post-Translational ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Viral Proteins ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2010-11-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01369-10
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Alphaherpesviral US3 kinase induces cofilin dephosphorylation to reorganize the actin cytoskeleton.

    Jacob, Thary / Van den Broeke, Céline / van Troys, Marleen / Waterschoot, Davy / Ampe, Christophe / Favoreel, Herman W

    Journal of virology

    2013  Volume 87, Issue 7, Page(s) 4121–4126

    Abstract: The conserved alphaherpesviral serine/threonine kinase US3 causes dramatic actin rearrangements, associated with increased viral spread. Here, we show that US3 of pseudorabies virus (PRV) leads to activation (dephosphorylation) of the central actin ... ...

    Abstract The conserved alphaherpesviral serine/threonine kinase US3 causes dramatic actin rearrangements, associated with increased viral spread. Here, we show that US3 of pseudorabies virus (PRV) leads to activation (dephosphorylation) of the central actin regulator cofilin. A mutation that impairs US3 kinase activity and the group I p21-activated kinase inhibitor IPA-3 inhibited US3-mediated cofilin activation. Additionally, expression of phosphomimetic S3D cofilin significantly suppressed the ability of US3 to cause cell projections and cell rounding. In conclusion, the US3 kinase of PRV leads to activation (dephosphorylation) of cofilin, and cofilin contributes to US3-mediated actin rearrangements.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actin Depolymerizing Factors/metabolism ; Blotting, Western ; Cell Shape/physiology ; Enzyme Inhibitors/metabolism ; Herpesvirus 1, Suid/enzymology ; Microscopy, Fluorescence ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Virus Internalization ; p21-Activated Kinases/antagonists & inhibitors
    Chemical Substances Actin Depolymerizing Factors ; Enzyme Inhibitors ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; p21-Activated Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2013-01-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.03107-12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Pseudorabies virus US3 leads to filamentous actin disassembly and contributes to viral genome delivery to the nucleus.

    Jacob, Thary / Van den Broeke, Céline / Grauwet, Korneel / Baert, Kim / Claessen, Christophe / De Pelsmaeker, Steffi / Van Waesberghe, Cliff / Favoreel, Herman W

    Veterinary microbiology

    2015  Volume 177, Issue 3-4, Page(s) 379–385

    Abstract: The conserved alphaherpesvirus US3 tegument protein induces rearrangements of the actin cytoskeleton, consisting of protrusion formation and stress fiber breakdown. Although US3 does not affect levels of total actin protein, it remains unclear whether ... ...

    Abstract The conserved alphaherpesvirus US3 tegument protein induces rearrangements of the actin cytoskeleton, consisting of protrusion formation and stress fiber breakdown. Although US3 does not affect levels of total actin protein, it remains unclear whether US3 modulates the total levels of filamentous (F) actin. In this report, we show that the pseudorabies virus (PRV) US3 protein, via its kinase activity, leads to disassembly of F-actin in porcine ST cells. F-actin disassembly has been reported before to contribute to host cell entry of HIV. In line with this, in the current study, we report that US3 has a previously uncharacterized role in viral genome delivery to the nucleus, since quantitative polymerase chain reaction (qPCR) assays on nuclear fractions demonstrated a reduced nuclear delivery of US3null PRV compared to wild type PRV genomes. Treatment of cells with the actin depolymerizing drug cytochalasin D enhanced virus genome delivery to the nucleus, particularly of US3null PRV, supporting a role for F-actin disassembly during certain aspects of viral entry. In conclusion, the US3 kinase of PRV leads to F-actin depolymerization, and US3 and F-actin disassembly contribute to viral genome delivery to the nucleus.
    MeSH term(s) Actin Cytoskeleton/metabolism ; Actin Cytoskeleton/ultrastructure ; Actins/metabolism ; Animals ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytochalasin D/pharmacology ; Genome, Viral/drug effects ; Herpesvirus 1, Suid/drug effects ; Herpesvirus 1, Suid/genetics ; Herpesvirus 1, Suid/physiology ; Male ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Pseudorabies/virology ; Rabbits ; Real-Time Polymerase Chain Reaction ; Swine ; Testis/cytology ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virion/genetics ; Virus Internalization
    Chemical Substances Actins ; Viral Proteins ; Cytochalasin D (22144-77-0) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2015-06-12
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 753154-0
    ISSN 1873-2542 ; 0378-1135
    ISSN (online) 1873-2542
    ISSN 0378-1135
    DOI 10.1016/j.vetmic.2015.03.023
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2917: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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