Shrimp Pm-fortilin inhibits the expression of early and late genes of white spot syndrome virus (WSSV) in an insect cell model

Nupan, Benjamas; Phongdara, Amornrat; Saengsakda, Manasawan; Leu, Jiann Horng; Lo, Chu Fang

doi:10.1016/j.dci.2010.11.016

Cited by 122 publications

(18 citation statements)

References 46 publications

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“…It has been reported that WSSV could 'infect' insect cells such as Sf 9 and S2, resulting in expression of some viral genes and replication of the viral genome, but no progeny virions could be detected in these cells (Chen et al, 2011;Nupan et al, 2011). A similar phenomenon has been observed in High Five (BTI-TN-5B1-4) cells.…”

supporting

confidence: 52%

Characterization of white spot syndrome virus immediate-early gene promoters

Lin

Huang

Wei

et al. 2013

Journal of General Virology

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Twenty-one immediate-early (IE) genes of white spot syndrome virus (WSSV) have been identified so far. However, the transcriptional regulation of WSSV IE genes remains largely unknown. In this report, the 59 flanking regions of 18 WSSV IE genes were cloned and eight functional promoter regions were identified. WSSV IE gene promoters normally contained a TATA box approximately 30 bp upstream of the transcriptional initiation site. Also, the cyclic AMP response element (CRE; TGACGTCA) was frequently found within the WSSV IE promoter regions. Mutations of the CREs of WSSV IE promoters P403 and P465 reduced their activity significantly, suggesting that these elements have a role in WSSV IE gene transcription. Our findings provide a more global view of WSSV IE gene promoters and will facilitate the in-depth investigation of viral gene transcriptional regulation.

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supporting

confidence: 52%

Characterization of white spot syndrome virus immediate-early gene promoters

Lin

Huang

Wei

et al. 2013

Journal of General Virology

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“…Subsequently, the same group demonstrated that injection of shrimps with recombinant TCTP/fortilin after infection with WSSV resulted in 80-100% survival, and it severely reduced the virus load (Tonganunt et al 2008). Consistent with this, TCTP/ fortilin of the shrimp Penaeus monodon inhibited the expression of early and late genes of the WSSV virus in an insect cell model (Nupan et al 2011). The group also identified a novel binding partner to TCTP/fortilin, fortilin-binding protein (FBP1), which might be involved in the immune defence as well (Panrat et al 2012).…”

Section: Tctp In Crustaceans and Other Waterborne Animalsmentioning

confidence: 73%

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Bommer

2017

Results and Problems in Cell Differentiation

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The Translational Controlled Tumour Protein TCTP (gene symbol TPT1, also called P21, P23, Q23, fortilin or histamine-releasing factor, HRF) is a highly conserved protein present in essentially all eukaryotic organisms and involved in many fundamental cell biological and disease processes. It was first discovered about 35 years ago, and it took an extended period of time for its multiple functions to be revealed, and even today we do not yet fully understand all the details. Having witnessed most of this history, in this chapter, I give a brief overview and review the current knowledge on the structure, biological functions, disease involvements and cellular regulation of this protein. TCTP is able to interact with a large number of other proteins and is therefore involved in many core cell biological processes, predominantly in the response to cellular stresses, such as oxidative stress, heat shock, genotoxic stress, imbalance of ion metabolism as well as other conditions. Mechanistically, TCTP acts as an anti-apoptotic protein, and it is involved in DNA-damage repair and in cellular autophagy. Thus, broadly speaking, TCTP can be considered a cytoprotective protein. In addition, TCTP facilitates cell division through stabilising the mitotic spindle and cell growth through modulating growth signalling pathways and through its interaction with the proteosynthetic machinery of the cell. Due to its activities, both as an anti-apoptotic protein and in promoting cell growth and division, TCTP is also essential in the early development of both animals and plants. Apart from its involvement in various biological processes at the cellular level, TCTP can also act as an extracellular protein and as such has been involved in modulating whole-body defence processes, namely in the mammalian immune system. Extracellular TCTP, typically in its dimerised form, is able to induce the release of cytokines and other signalling molecules from various types of immune cells. There are also several examples, where TCTP was shown to be involved in antiviral/antibacterial defence in lower animals. In plants, the protein appears to have a protective effect against phytotoxic stresses, such as flooding, draught, too high or low temperature, salt stress or exposure to heavy metals. The finding for the latter stress condition is corroborated by earlier reports that TCTP levels are considerably up-regulated upon exposure of earthworms to high levels of heavy metals. Given the involvement of TCTP in many biological processes aimed at maintaining cellular or whole-body homeostasis, it is not surprising that dysregulation of TCTP levels may promote a range of disease processes, foremost cancer. Indeed a large body of evidence now supports a role of TCTP in at least the most predominant types of human cancers. Typically, this can be ascribed to both the anti-apoptotic activity of the protein and to its function in promoting cell growth and division. However, TCTP also appears to be involved in the later stages of cancer progression, such ...

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“…The Sf9 cell line from Spodoptera frugiperda, a lepidopteran insect, has been reported to support WSSV replication (22). To further analyze whether the FcUbc could ubiquitinate the WRD-containing proteins in the WSSV, we performed WSSV infection in Drosophila S2 cells and obtained reasonable results.…”

Section: Discussionmentioning

confidence: 99%

“…To further investigate the influence of FcUbc on WRD-containing proteins during WSSV infection, S2 cells were utilized to perform WSSV infection following the methods reported by Nupan et al (22). Cells were incubated with WSSV or UV-treated WSSV for 4 h before washing and medium replacement and collected at 24 h, 48 h, 72 h, and 96 h postinfection.…”

Section: Methodsmentioning

confidence: 99%

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

Chen

Wang

Zhao

et al. 2011

J Virol

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Recent studies have shown that the ubiquitin (Ub) proteasome pathway (UPP) is closely related to immune defense. We have identified a ubiquitin-conjugating enzyme, E2, from the Chinese white shrimp, Fenneropenaeus chinensis (FcUbc). Injection of recombinant FcUbc protein (rFcUbc) reduced the mortality of shrimp infected with white spot syndrome virus (WSSV) and inhibited replication of WSSV. rFcUbc, but not a mutant FcUbc (mFcUbc), bound to WSSV RING domains (WRDs) from four potential E3 ligase proteins of WSSV in vitro. Importantly, rFcUbc could ubiquitinate the RING domains (named WRD2 and WRD3) of WSSV277 and WSSV304 proteins in vitro and the two proteins in WSSV-infected Drosophila melanogaster Schneider 2 (S2) cells. Furthermore, overexpression of FcUbc increased ubiquitination of WSSV277 and WSSV304 during WSSV infection. In summary, our study demonstrates that FcUbc from Chinese white shrimp inhibited WSSV replication and could ubiquitinate WSSV RING domain-containing proteins. This is the first report about antiviral function of Ubc E2 in shrimp.

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Shrimp Pm-fortilin inhibits the expression of early and late genes of white spot syndrome virus (WSSV) in an insect cell model

Cited by 122 publications

References 46 publications

Characterization of white spot syndrome virus immediate-early gene promoters

Characterization of white spot syndrome virus immediate-early gene promoters

The Translational Controlled Tumour Protein TCTP: Biological Functions and Regulation

Enzyme E2 from Chinese White Shrimp Inhibits Replication of White Spot Syndrome Virus and Ubiquitinates Its RING Domain Proteins

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