Transcriptional induction of the ubiquitin gene during herpes simplex virus infection is dependent upon the viral immediate-early protein ICP4

Latchman, David S.; Estridge, J K; Kemp, L.M.

doi:10.1093/nar/15.18.7283

Cited by 43 publications

(24 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We next considered the relevance of the results described above to ICP0 function during the early stages of HSV-1 infection. Since virus infection induces a stress response and expression of ICP4 has been shown to induce transcription of a ubiquitin precursor gene (32), it was first necessary to assess the effect of HSV-1 infection on the distribution of conjugated ubiquitin by using an ICP0-deficient virus. Mutant vEG-dl110 expresses EGFP from the IE-1 promoter in place of ICP0 (33) and is therefore very convenient for these experiments, since it is ICP0 negative and expresses EGFP at IE times.…”

Section: Icp0 Induces Colocalization Of Conjugated Ubiquitinmentioning

confidence: 99%

ICP0 Induces the Accumulation of Colocalizing Conjugated Ubiquitin

Everett¹

2000

J Virol

109

View full text Add to dashboard Cite

Herpes simplex virus type 1 (HSV-1) immediate-early protein ICP0 is a general activator of viral gene expression which stimulates the initiation of lytic infection and reactivation from quiescence and latency. The importance of ICP0 to the biology of HSV-1 infection has stimulated interest in its mode of action. Previous studies have reported its interactions with other viral regulatory molecules, with the translation apparatus, with cyclin D3, and with a ubiquitin-specific protease. It has been demonstrated that ICP0 is able to induce the proteasome-dependent degradation of a number of cellular proteins, including components of centromeres and small nuclear substructures known as ND10 or PML nuclear bodies. ICP0 has a RING finger zinc-binding domain which is essential for its functions. In view of several recent examples of other RING finger proteins which modulate the stability of specific target proteins by acting as components of E3 ubiquitin ligase complexes, this study has explored whether ICP0 might operate via a similar mechanism. Evidence that the foci of accumulated ICP0 in transfected and infected cells contain enhanced levels of conjugated ubiquitin is presented. This effect was dependent on the RING finger region of ICP0, and comparison of the properties of a number of ICP0 mutants revealed an excellent correlation between previously established functions of ICP0 and its ability to induce concentrations of colocalizing conjugated ubiquitin. These results strongly support the hypothesis that a major factor in the mechanism by which ICP0 influences virus infection is its ability to induce the degradation of specific cellular targets by interaction with the ubiquitin-proteasome pathway.A definitive feature of herpes simplex virus type 1 (HSV-1) is the contrast between episodic lytic infection in the epithelia and periods of latency when the viral genome resides in a mainly quiescent state in neurons (for general reviews, see reference 22). Lytic infection involves the initial synthesis of immediate-early (IE) regulatory proteins: ICP4 functions at the level of transcription by interacting with components of the basal transcription apparatus (4), ICP27 is a multifunctional protein which acts at both the transcriptional and posttranscriptional levels (reviewed in reference 45), ICP22 enhances levels of late gene expression in selected cell types (49), and ICP0 enhances gene expression from all classes of viral genes (reviewed in references 11 and 13). The combined activities of the IE proteins lead to transcription of the early and late classes of genes throughout the whole viral genome. In contrast, abundant transcription during latency is limited to the family of latency-associated transcripts of uncertain function (reviewed in reference 55).Attempts to understand the basis of the contrasting patterns of viral transcription during lytic and latent infection have concentrated on the properties of the IE regulatory proteins. ICP0 was originally defined as a promiscuous activator of gene expression in tra...

show abstract

Section: Icp0 Induces Colocalization Of Conjugated Ubiquitinmentioning

confidence: 99%

ICP0 Induces the Accumulation of Colocalizing Conjugated Ubiquitin

Everett¹

2000

J Virol

109

View full text Add to dashboard Cite

show abstract

“…Despite the HSV-1-induced shutoff of most host protein synthesis, a few cellular proteins are still synthesized after infection (Estridge et al, 1989 ;Everett, 1985 ;Kemp & Latchman, 1988 a, b ;Latchman et al, 1987 ;Mosca et al, 1992 ;Notarianni & Preston, 1982 ;Preston, 1990). The sustained synthesis of some cellular proteins suggests they might play an important role in virus-cell interactions, in particular in determining the outcome of infection.…”

Section: Introductionmentioning

confidence: 99%

Persistence of ribosomal protein synthesis after infection of HeLa cells by herpes simplex virus type 1.

Simonin

Diaz

Massé

et al. 1997

Journal of General Virology

View full text Add to dashboard Cite

Because synthesis of rRNA persists late during herpes simplex type 1 infection and because S6 phosphorylation is always correlated with efficient translation of ribosomal protein mRNA, we tested the hypothesis that ribosomal protein synthesis and ribosome biogenesis could persist after infection. At different times after infection, proteins were labelled with 35 S for 1 h before harvesting and ribosomes were purified. Measurement of radioactivity incorporated into individual ribosomal proteins separated by two-dimensional PAGE demonstrated that ribosomal proteins are still synthesized and assembled into mature ribosomes up to late times during infection, while synthesis of

show abstract

“…The upregulation of PmUbc at 24 hpi in WSSV challenged shrimp was revealed using semi-quantitative and real time PCR [16]. Many findings have shown that viral infection can up-regulate expression of ubiquitin [19,18], suggesting that the ubiquitin system may play a key role in the course of viral infection. Therefore, the present study reveals the expression patterns of PmUbc at protein level in WSSV infected P. monodon.…”

Section: Discussionmentioning

confidence: 99%

Expression Profile of Penaeus monodon Ubiquitin Conjugating Enzyme (PmUbc) at Protein Level in White spot syndrome virus Challenged Shrimp

et al. 2013

View full text Add to dashboard Cite

White spot syndrome virus (WSSV) is one of the major pathogens in shrimp aquaculture. Four proteins of WSSV are predicted to encode a RING H2 domain, which in presence of ubiquitin conjugating enzyme (E2) in shrimps can function as viral E3 ligase and modulate the host ubiquitin proteasome pathway. Modulation of host ubiquitin proteasome pathway by viral proteins is implicated in viral pathogenesis. In the present study, expression profile of Penaeus monodon Ubiquitin conjugating enzyme (PmUbc) was studied at protein level in WSSV challenged shrimp. A time point analysis of the expression of PmUbc was carried out at 0, 3, 6, 12, 24, 48 and 72 h post WSSV challenge in P. monodon. Recombinant PmUbc (rPmUbc) was produced in prokaryotic expression vector, BL21 (DE3) pLys S. The PmUbc expression pattern was studied by ELISA with rPmUbc antibodies raised in rabbit. A significant increase in PmUbc expression at 24 h post infection (hpi) was observed followed by a decline till 72 hpi. Since the up-regulation and a tremendous decline of PmUbc protein expression was observed at 24 and in 72 hpi respectively in ELISA, it can be speculated that these proteins might interact with host ubiquitination pathway for viral pathogenesis. Many findings have shown that viral infection can up-regulate expression of ubiquitin and that the ubiquitin system plays a key role in the course of viral infection. The present study reveals the expression patterns of PmUbc at protein level in WSSV infected P. monodon. However, further studies are to be carried out to unfold the molecular mechanism of interaction between host and virus to devise efficient control strategies for this major culprit in shrimp culture industry.

show abstract

Transcriptional induction of the ubiquitin gene during herpes simplex virus infection is dependent upon the viral immediate-early protein ICP4

Cited by 43 publications

References 44 publications

ICP0 Induces the Accumulation of Colocalizing Conjugated Ubiquitin

ICP0 Induces the Accumulation of Colocalizing Conjugated Ubiquitin

Persistence of ribosomal protein synthesis after infection of HeLa cells by herpes simplex virus type 1.

Expression Profile of Penaeus monodon Ubiquitin Conjugating Enzyme (PmUbc) at Protein Level in White spot syndrome virus Challenged Shrimp

Contact Info

Product

Resources

About