An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif

Crook, Norman E.; Clem, Rollie J.; Miller, Lois K.

doi:10.1128/jvi.67.4.2168-2174.1993

Cited by 925 publications

(307 citation statements)

References 35 publications

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“…7) may be due to expression of iap-like genes documented in the CIV genome, viz ORF 157L (L), ORF 193R (IDL), ORF 332L (IL), and ORF 284R (L) (Jakob et al, 2001;D'Costa et al, 2004). The first three of these ORFs are similar to iap genes in Cydia pomonella granulosis virus (CpGV; (Crook et al, 1993) and have the following motifs, respectively: ring finger, BIR repeat profile, and bipartite nuclear localization signal. ORF 284R is similar to an ASFV gene coding for a polypeptide (p27) with an IAP domain (Chacon et al, 1995) and is expressed exclusively at late times in CIV infections (D'Costa et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Modulation of iridovirus-induced apoptosis by endocytosis, early expression, JNK, and apical caspase

et al. 2008

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Chilo iridescent virus (CIV) is the type species for the family Iridoviridae, which are large, isometric, cytoplasmic dsDNA viruses. We examined the mechanism of apoptosis induction by CIV. High CIV doses (CIV(XS); 400 microg/ml), UV-irradiated virus (CIV(UV); 10 microg/ml) and CVPE (CIV protein extract; 10 microg/ml) induced apoptosis in 60% of treated Choristoneura fumiferana (IPRI-CF-124T) cells. Normal doses of infectious CIV (10 microg/ml) induced apoptosis in only 10% of C. fumiferana (CF) cells. Apoptosis was inhibited by Z-IETD-FMK, an apical caspase inhibitor, indicating that CIV-induced apoptosis requires caspase activity. The putative caspase in CF cells was designated Cf-caspase-i. CIV(UV) or CVPE enhanced Cf-caspase-i activity by 80% at 24 h relative to mock-treated cells. Since the MAP kinase pathway induces or inhibits apoptosis depending on the context, we used JNK inhibitor SP600125 and demonstrated drastic suppression of CVPE-induced apoptosis. Thus, the JNK signaling pathway is significant for apoptosis in this system. Virus interaction with the cell surface was not sufficient for apoptosis since CIV(UV) particles bound to polysterene beads failed to induce apoptosis. Endocytosis inhibitors (bafilomycin or ammonium chloride) negated apoptosis induction by CIV(UV), CIV(XS) or CVPE indicating that entry through this mode is required. Given the weak apoptotic response to infectious CIV, we postulated that viral gene expression inhibited apoptosis. CIV infection of cells pretreated with cycloheximide induced apoptosis in 69% of the cells compared to 10% in normal infections. Furthermore, blocking viral DNA replication with aphidicolin or phosphonoacetic acid suppressed apoptosis and Cf-caspase-i activity, indicating that early viral expression is necessary for inhibition of apoptosis, and de novo synthesis of viral proteins is not required for induction. We show for the first time that, in a member of the family Iridoviridae, apoptosis: (i) requires entry and endocytosis of virions or virion proteins, (ii) is inhibited under conditions permitting early viral expression, and (iii) requires the JNK signaling pathway. This is the first report of JNK signal requirement during apoptosis induction by an insect virus.

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Section: Discussionmentioning

confidence: 99%

Modulation of iridovirus-induced apoptosis by endocytosis, early expression, JNK, and apical caspase

et al. 2008

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“…Studies on the regulation of insect cell death induced by baculovirus that lacked a functional p35 gene led to the discovery of another potent inhibitor of apoptosis, IAP. The protein is characterized by a small (∼ 70-80 residues), highly conserved Zn 2+ -binding module termed the BIR (baculoviral IAP repeat) [244]. Endogenous homologues of IAP were identified shortly afterwards in animals [245][246][247][248], with eight members characterized to date in humans (reviewed in [249][250][251]).…”

Section: Xiap: a Non-standard Design For A Very Specific Caspase Inhimentioning

confidence: 99%

The protein structures that shape caspase activity, specificity, activation and inhibition

Fuentes‐Prior

Salvesen

2004

Biochemical Journal

760

713

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The death morphology commonly known as apoptosis results from a post-translational pathway driven largely by specific limited proteolysis. In the last decade the structural basis for apoptosis regulation has moved from nothing to 'quite good', and we now know the fundamental structures of examples from the initiator phase, the pre-mitochondrial regulator phase, the executioner phase, inhibitors and their antagonists, and even the structures of some substrates. The field is as well advanced as the best known of proteolytic pathways, the coagulation cascade. Fundamentally new mechanisms in protease regulation have been disclosed. Structural evidence suggests that caspases have an unusual catalytic mechanism, and that they are activated by apparently unrelated events, depending on which position in the apoptotic pathway they occupy. Some naturally occurring caspase inhibitors have adopted classic inhibition strategies, but other have revealed completely novel mechanisms. All of the structural and mechanistic information can, and is, being applied to drive therapeutic strategies to combat overactivation of apoptosis in degenerative disease, and underactivation in neoplasia. We present a comprehensive review of the caspases, their regulators and inhibitors from a structural and mechanistic point of view, and with an aim to consolidate the many threads that define the rapid growth of this field.

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“…However, some viruses evolve strategies to evade early apoptosis in order to avoid the elimination of progeny virus spread and the limitation of virus production [55]. For instance, an inhibitor of apoptosis proteins (IAPs), a family of proteins which were originally discovered in baculovirus has been reported to be involved in suppressing the host cell death in response to viral infection [57,58]. Protein kinases C (PKC) family members are associated with an extensive range of cellular responses including cell permeability, migration, hypertrophy, proliferation, secretion, and also apoptosis.…”

Section: Phosphorylation May Regulate Anti-apoptotic Cells Through Thmentioning

confidence: 99%

Quantitative phosphoproteome on the silkworm (Bombyx mori) cells infected with baculovirus

Shobahah

Xue

et al. 2017

Virol J

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Background Bombyx mori has become an important model organism for many fundamental studies. Bombyx mori nucleopolyhedrovirus (BmNPV) is a significant pathogen to Bombyx mori, yet also an efficient vector for recombinant protein production. A previous study indicated that acetylation plays many vital roles in several cellular processes of Bombyx mori while global phosphorylation pattern upon BmNPV infection remains elusive.MethodEmploying tandem mass tag (TMT) labeling and phosphorylation affinity enrichment followed by high-resolution LC-MS/MS analysis and intensive bioinformatics analysis, the quantitative phosphoproteome in Bombyx mori cells infected by BmNPV at 24 hpi with an MOI of 10 was extensively examined.ResultsTotally, 6480 phosphorylation sites in 2112 protein groups were identified, among which 4764 sites in 1717 proteins were quantified. Among the quantified proteins, 81 up-regulated and 25 down-regulated sites were identified with significant criteria (the quantitative ratio above 1.3 was considered as up-regulation and below 0.77 was considered as down-regulation) and with significant p-value (p < 0.05). Some proteins of BmNPV were also hyperphosphorylated during infection, such as P6.9, 39 K, LEF-6, Ac58-like protein, Ac82-like protein and BRO-D.ConclusionThe phosphorylated proteins were primary involved in several specific functions, out of which, we focused on the binding activity, protein synthesis, viral replication and apoptosis through kinase activity.

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An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif

Cited by 925 publications

References 35 publications

Modulation of iridovirus-induced apoptosis by endocytosis, early expression, JNK, and apical caspase

Modulation of iridovirus-induced apoptosis by endocytosis, early expression, JNK, and apical caspase

The protein structures that shape caspase activity, specificity, activation and inhibition

Quantitative phosphoproteome on the silkworm (Bombyx mori) cells infected with baculovirus

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