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Vishva M Dixit - One of the best experts on this subject based on the ideXlab platform.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Shimin Hu, Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Abstract Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1β-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1beta-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

Claudius Vincenz - One of the best experts on this subject based on the ideXlab platform.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Shimin Hu, Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Abstract Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1β-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1beta-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

Mark Buller - One of the best experts on this subject based on the ideXlab platform.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Shimin Hu, Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Abstract Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1β-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1beta-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

Shimin Hu - One of the best experts on this subject based on the ideXlab platform.

  • a novel family of viral death effector domain containing molecules that inhibit both cd 95 and tumor necrosis factor receptor 1 induced apoptosis
    Journal of Biological Chemistry, 1997
    Co-Authors: Shimin Hu, Claudius Vincenz, Mark Buller, Vishva M Dixit
    Abstract:

    Abstract Molluscum contagiosum virus proteins MC159 and MC160 and the Equine Herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1β-converting enzyme (FLICE) (caspase-8). FADD and FLICE participate in generating the death signal from both tumor necrosis factor receptor-1 (TNFR-1) and the CD-95 receptor. The flow of death signals from TNFR-1 occurs through the adaptor molecule tumor necrosis factor receptor-associated death domain protein (TRADD) to FADD to FLICE, whereas for CD-95 the receptor directly communicates with FADD and then FLICE. MC159 and E8 inhibited both TNFR-1- and CD-95-induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD. Neither viral molecule, however, inhibited FLICE-induced killing, consistent with an inhibitory action upstream of the active death protease. These data suggest the existence of a novel strategy employed by viruses to attenuate host immune killing mechanisms. Given that bovine Herpesvirus 4 protein E1.1 and Kaposi's sarcoma associated-Herpesvirus protein K13 also possess significant homology to the viral inhibitory molecules MC159, MC160, and E8, it may be that this class of proteins is used ubiquitously by viruses to evade host defense.

Kerstin Borchers - One of the best experts on this subject based on the ideXlab platform.

  • the mouse is not permissive for Equine Herpesvirus 2 ehv 2 however viral dna persisted in lung and spleen depending on the inoculation route
    Archives of Virology, 2002
    Co-Authors: Kerstin Borchers, J Brackmann, O Kershaw
    Abstract:

    BALB/c mice were inoculated with 3 EHV-2 low passage isolates. After intranasal inoculation, viral DNA was detected by virus-specific nested PCR in the lung up to day 30 post inoculation and in nasal turbinates till day 7. In trigeminal ganglia, olfactory bulb, brain and lymph nodes viral DNA was randomly shown by PCR. After intraperitoneal inoculation viral DNA was present in lymphoid tissues. The spleen was PCR positive up to day 30 and showed a splenomegaly. Clinical signs, virus replication and viraemia, were not observed and no virus strain-specific differences were obvious. Control mice inoculated with Equine Herpesvirus 4 were PCR negative in all tissues.

  • detection and distribution of Equine Herpesvirus 2 dna in the central and peripheral nervous systems of ponies
    Journal of General Virology, 1997
    Co-Authors: S M Rizvi, J. D. Slater, U Wolfinger, Kerstin Borchers, H J Field, A.j. Slade
    Abstract:

    The distribution of Equine Herpesvirus 2 (EHV-2) DNA within neurological and lymphoid tissues from 12 EHV-2 seropositive Welsh mountain ponies was determined by PCR. The lymphoid sites sampled in this study were almost universally PCR positive, thus confirming the existing virus co-cultivation data which suggest that the lymph nodes draining the respiratory tract are the main reservoirs of EHV-2 DNA. In addition, EHV-2 DNA was also detected, albeit with lower frequency, within both the peripheral and central nervous systems (PNS and CNS) of these animals. Of the CNS sites sampled 11% were PCR-positive and in the PNS the trigeminal ganglion proved PCR-positive in 50% of the animals tested. Since the nasal epithelium is innervated by the maxillary division of the trigeminal nerve, these observations suggest that the trigeminal ganglion may represent a biologically important site for EHV-2 latency.