Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.

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Ressource 1Télécharger: BIB_0C9041508C29.P001.pdf (2533.71 [Ko])
Etat: Serval
Version: de l'auteur
ID Serval
serval:BIB_0C9041508C29
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.
Périodique
Nature
Auteur(s)
Thome M., Schneider P., Hofmann K., Fickenscher H., Meinl E., Neipel F., Mattmann C., Burns K., Bodmer J.L., Schröter M., Scaffidi C., Krammer P.H., Peter M.E., Tschopp J.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Statut éditorial
Publié
Date de publication
1997
Volume
386
Numéro
6624
Pages
517-521
Langue
anglais
Résumé
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.
Mots-clé
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
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:18
Dernière modification de la notice
08/05/2019 14:20
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