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- W161560433 abstract "Caspase-dependent apoptosis has an important role in controlling viruses, and as a result, viruses often encode proteins that target this pathway. Caspase-dependent apoptosis can be activated from within the infected cell as an intrinsic response to replication-associated stresses or through death-inducing signals produced extrinsically by immune cells. Cytomegaloviruses (CMVs) encode a mitochondria-localized inhibitor of apoptosis, vMIA, and a viral inhibitor of caspase activation, vICA, the functional homologs of Bcl-2 related and c-FLIP proteins, respectively. Evidence from viral mutants deleting either vMIA or vICA suggests that each is necessary and sufficient to promote survival of infected cells undergoing caspase-dependent apoptosis. Additional proteins, including pUL38, IE1(491a), and IE2(579aa), can prevent apoptosis induced by various stimuli, while viruses with deletions of UL38, M45, or m41 undergo apoptosis. The viral RNA, beta2.7, binds mitochondrial respiratory complex I, maintains ATP production late in infection, and prevents death induced by a mitochondrial poison. Thus, CMV alters cell intrinsic defenses employing apoptosis, and multiple viral gene products together control death-inducing stimuli to promote survival." @default.
- W161560433 created "2016-06-24" @default.
- W161560433 creator A5077319683 @default.
- W161560433 date "2008-01-01" @default.
- W161560433 modified "2023-10-14" @default.
- W161560433 title "Control of Apoptosis by Human Cytomegalovirus" @default.
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- W161560433 doi "https://doi.org/10.1007/978-3-540-77349-8_16" @default.
- W161560433 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18637512" @default.
- W161560433 hasPublicationYear "2008" @default.
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