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Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.
Viruses have evolved many distinct strategies to avoid the host's apoptotic response. Here we describe a new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors and which are present in several gamma-herpesviruses (including Kaposi's-sarcoma-associated human herpesvirus-8), as well as in the tumorigenic human molluscipoxvirus. v-FLIPs contain two death-effector domains which interact with the adaptor protein FADD, and this inhibits the recruitment and activation of the protease FLICE by the CD95 death receptor. Cells expressing v-FLIPs are protected against apoptosis induced by CD95 or by the related death receptors TRAMP and TRAIL-R. The herpesvirus saimiri FLIP is detected late during the lytic viral replication cycle, at a time when host cells are partially protected from CD95-ligand-mediated apoptosis. Protection of virus-infected cells against death-receptor-induced apoptosis may lead to higher virus production and contribute to the persistence and oncogenicity of several FLIP-encoding viruses.
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antigens, CD95/metabolism, Apoptosis, Apoptosis Regulatory Proteins, Carrier Proteins/metabolism, Caspase 8, Caspase 9, Caspases, Cell Line, Cell Transformation, Viral, Cysteine Endopeptidases/metabolism, Fas-Associated Death Domain Protein, Gammaherpesvirinae/genetics, Gammaherpesvirinae/physiology, Herpesvirus 2, Saimiriine/physiology, Humans, Membrane Glycoproteins/metabolism, Mice, Molecular Sequence Data, Receptors, Tumor Necrosis Factor/metabolism, Receptors, Tumor Necrosis Factor, Member 25, Sequence Homology, Amino Acid, Signal Transduction, TNF-Related Apoptosis-Inducing Ligand, Tumor Necrosis Factor-alpha/metabolism, Viral Proteins/physiology, Virus Replication
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