NDLI: Cell death suppression by cytomegaloviruses

Please wait, while we are loading the content...

Procaspase-2S inhibits procaspase-3 processing and activation, preventing ROCK-1-mediated apoptotic blebbing and body formation in human B lymphoma Namalwa cells

Structure-based design of an agonistic peptide targeting Fas

Analysis of gene expression in apoptosis of human lymphoma U937 cells induced by heat shock and the effects of α-phenyl N-tert-butylnitrone (PBN) and its derivatives

Phosphorylation of Bad is not essential for PKB-mediated survival signaling in hemopoietic cells

Fenofibrate induces apoptotic injury in cultured human hepatocytes by inhibiting phosphorylation of Akt

α-lipoic acid induces apoptosis in human colon cancer cells by increasing mitochondrial respiration with a concomitant O2−.-generation

Zinc pyrithione induces apoptosis and increases expression of Bim

Iron deprivation induces apoptosis via mitochondrial changes related to Bax translocation

Apoptosis and cell removal in the cryptorchid rat testis

ER stress-induced caspase-12 activation is inhibited by PKC in neuronal cells

Structural and functional preservation of specific sequences of DNA and mRNA in apoptotic bodies from ES cells

A novel time resolved fluorometric assay of anoikis using Europium-labelled Annexin V in cultured adherent cells

Recruitment of beta-2-glycoprotein 1 to cell surfaces in extrinsic and intrinsic apoptosis

Stochastic modelling of apoptosis kinetics

Apoptosis : Volume 10, Issue 1, January 2005

Cell death suppression by cytomegaloviruses

Content Provider	Springer Nature Link
Author	Goldmacher, V. S.
Copyright Year	2005
Abstract	Cytomegaloviruses (CMVs), a subset of betaherpesviruses, employ multiple strategies to suppress apoptosis in infected cells and thus to delay their death. Human cytomegalovirus (HCMV) encodes at least two proteins that directly interfere with the apoptotic signaling pathways, viral inhibitor of caspase-8-induced apoptosis vICA (pUL36), and mitochondria-localized inhibitor of apoptosis vMIA (pUL37 × 1). vICA associates with pro-caspase-8 and appears to block its recruitment to the death-inducing signaling complex (DISC), a step preceding caspase-8 activation. vMIA binds and sequesters Bax at mitochondria, and interferes with BH3-only-death-factor/Bax-complex-mediated permeabilization of mitochondria. vMIA does not seem to either interact with Bak, a close structural and functional homologue of Bax, or to suppress Bak-mediated permeabilization of mitochondria and Bak-mediated apoptosis. All sequenced betaherpesviruses, including CMVs, encode close homologues of vICA, and those vICA homologues that have been tested, were found to be functional cell death suppressors. Overt sequence homologues of vMIA were found only in the genomes of primate CMVs, but recent observations made with murine CMV (MCMV) indicate that non-primate CMVs may also encode a cell death suppressor functionally resembling vMIA. The exact physiological rolesand relative contributions of vMIA and vICA in suppressing death of CMV-infected cells in vivo have not been elucidated. There is strong evidence that the cell death suppressing function of vMIA is indispensable, and that vICA is dispensable for replication of HCMV. In addition to suppressed caspase-8 activation and sequestered Bax, CMV-infected cells display several other phenomena, less well characterized, that may diminish, directly or indirectly the extent of cell death.
Starting Page	251
Ending Page	265
Page Count	15
File Format	PDF
ISSN	13608185
Journal	Apoptosis
Volume Number	10
Issue Number	2
e-ISSN	1573675X
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	alphaherpesvirus apoptosis Bak Bax Bcl-2 betaherpesvirus caspase-8 cell death suppressor cytomegalovirus gammaherpesvirus herpesvirus inhibitor of apoptosis programmed cell death vICA vMIA Cancer Research Virology Oncology Biochemistry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Pharmaceutical Science Biochemistry (medical) Cell Biology Clinical Biochemistry Cancer Research Pharmacology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The murine cytomegalovirus cell death suppressor m38.5 binds Bax and blocks Bax-mediated mitochondrial outer membrane permeabilization

Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria

Herpesvirus infections of laboratory macaques

Contribution of GADD45 family members to cell death suppression by cellular Bcl-xL and cytomegalovirus vMIA

Bcl-2 and Bax mammalian regulators of apoptosis are functional in Drosophila

Betulinic acid induces cytochrome c release and apoptosis in a Bax/Bak-independent, permeability transition pore dependent fashion

Betulinic acid induces cytochrome c release and apoptosis in a Bax/Bak-independent, permeability transition pore dependent fashion

The BH3 α-Helical Mimic BH3-M6 Disrupts Bcl-XL, Bcl-2, and MCL-1 Protein-Protein Interactions with Bax, Bak, Bad, or Bim and Induces Apoptosis in a Bax- and Bim-dependent Manner

Die Another Day: Inhibition of Cell Death Pathways by Cytomegalovirus

Cell death suppression by cytomegaloviruses

Similar Documents

The murine cytomegalovirus cell death suppressor m38.5 binds Bax and blocks Bax-mediated mitochondrial outer membrane permeabilization

Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria

Herpesvirus infections of laboratory macaques

Contribution of GADD45 family members to cell death suppression by cellular Bcl-xL and cytomegalovirus vMIA

Bcl-2 and Bax mammalian regulators of apoptosis are functional in Drosophila

Betulinic acid induces cytochrome c release and apoptosis in a Bax/Bak-independent, permeability transition pore dependent fashion

Betulinic acid induces cytochrome c release and apoptosis in a Bax/Bak-independent, permeability transition pore dependent fashion

The BH3 α-Helical Mimic BH3-M6 Disrupts Bcl-XL, Bcl-2, and MCL-1 Protein-Protein Interactions with Bax, Bak, Bad, or Bim and Induces Apoptosis in a Bax- and Bim-dependent Manner

Die Another Day: Inhibition of Cell Death Pathways by Cytomegalovirus

Cell death suppression by cytomegaloviruses