Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1997-04

AUTHORS

Margot Thome, Pascal Schneider, Kay Hofmann, Helmut Fickenscher, Edgar Meinl, Frank Neipel, Chantal Mattmann, Kim Burns, Jean-Luc Bodmer, Michael Schröter, Carsten Scaffidi, Peter H. Krammer, Marcus E. Peter, Jürg Tschopp

ABSTRACT

Viruses have evolved many distinct strategies to avoid the host's apoptotic response1,2. Here we describe a new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors3 and which are present in several γ-herpesviruses (including Kaposi's-sarcoma-associated human herpesvirus-8), as well as in the tumorigenic human molluscipoxvirus4. v-FLIPs contain two death-effector domains which interact with the adaptor protein FADD5,6, and this inhibits the recruitment and activation of the protease FLICE7,8 by the CD95 death receptor3. Cells expressing v-FLIPs are protected against apoptosis induced by CD95 or by the related death receptors TRAMP9–12 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 oncogenicity13 of several FLIP-encoding viruses. More... »

PAGES

517-521

Journal

TITLE

Nature

ISSUE

6624

VOLUME

386

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/386517a0

DOI

http://dx.doi.org/10.1038/386517a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021049959

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9087414


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39 schema:description Viruses have evolved many distinct strategies to avoid the host's apoptotic response1,2. Here we describe a new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors3 and which are present in several γ-herpesviruses (including Kaposi's-sarcoma-associated human herpesvirus-8), as well as in the tumorigenic human molluscipoxvirus4. v-FLIPs contain two death-effector domains which interact with the adaptor protein FADD5,6, and this inhibits the recruitment and activation of the protease FLICE7,8 by the CD95 death receptor3. Cells expressing v-FLIPs are protected against apoptosis induced by CD95 or by the related death receptors TRAMP9–12 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 oncogenicity13 of several FLIP-encoding viruses.
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