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- Title
Viral Bcl2s' transmembrane domain interact with host Bcl2 proteins to control cellular apoptosis.
- Authors
García-Murria, Maria Jesús; Duart, Gerard; Grau, Brayan; Diaz-Beneitez, Elisabet; Rodríguez, Dolores; Mingarro, Ismael; Martínez-Gil, Luis
- Abstract
Viral control of programmed cell death relies in part on the expression of viral analogs of the B-cell lymphoma 2 (Bcl2) protein known as viral Bcl2s (vBcl2s). vBcl2s control apoptosis by interacting with host pro- and anti-apoptotic members of the Bcl2 family. Here, we show that the carboxyl-terminal hydrophobic region of herpesviral and poxviral vBcl2s can operate as transmembrane domains (TMDs) and participate in their homo-oligomerization. Additionally, we show that the viral TMDs mediate interactions with cellular pro- and anti-apoptotic Bcl2 TMDs within the membrane. Furthermore, these intra-membrane interactions among viral and cellular proteins are necessary to control cell death upon an apoptotic stimulus. Therefore, their inhibition represents a new potential therapy against viral infections, which are characterized by short- and long-term deregulation of programmed cell death. Viral analogs of B-cell lymphoma 2 (Bcl2), known as vBcl2s, control apoptosis by interacting with host pro- and anti-apoptotic members of the Bcl2 family. Here, García-Murria et al. report on transmembrane domains (TMDs) in the C-terminal hydrophobic region of herpes- and poxviral vBcl2s, which mediate homo-oligomerization and interactions with cellular Bcl2 TMDs to control apoptosis.
- Subjects
VIRAL proteins; CELL death; VIRUS diseases; PROTEINS; PROGRAMMED cell death 1 receptors
- Publication
Nature Communications, 2020, Vol 11, Issue 1, pN.PAG
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-020-19881-9