Heliocoverpa armigera single nucleocapsid nucleopolyhedrovirus induces Hz-AM1 cell cycle arrest at the G2 phase with accumulation of cyclin B1

Zhou, Rui; Yu, Ze-Hua; Li, Xiaoqing; Jia, Fang; Wu, Jianhong; Chen, Xinwen

doi:10.1016/j.virusres.2004.05.001

Cited by 13 publications

(18 citation statements)

References 25 publications

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“…Error bars indicate standard deviations (n ϭ 3). arrest insect cell lines in the G 2 /M and S phases, induced by viral genes ie1 and ie2, and resulting in enlarged cells with high quantities of viral DNA (7,51,67). In our study, genes related to cell cycle and cell cycle arrest, namely, cyclin B homolog, cullin-1, and 14-3-3 epsilon, were downregulated immediately after BmNPV infection.…”

Section: Discussionsupporting

confidence: 46%

“…A cyclin B homolog, which was also predicted to interact with viral proteins, was immediately downregulated after BmNPV infection in our study. In contrast, Zhou et al (67) have shown that a significant increase in cyclin B1 is able to induce cell cycle arrest at the G 2 phase. During G 2 , cyclin B1 can accumulate and form a kinase complex with Cdk1.…”

Section: Discussionmentioning

confidence: 86%

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Dynamic Interactions between Bombyx mori Nucleopolyhedrovirus and Its Host Cells Revealed by Transcriptome Analysis

Xue

Qiao

Zhang

et al. 2012

J Virol

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Although microarray and expressed sequence tag (EST)-based approaches have been used to profile gene expression during baculovirus infection, the response of host genes to baculovirus infection and the interaction between baculovirus and its host remain largely unknown. To determine the host response to Bombyx mori nucleopolyhedrovirus infection and the dynamic interaction between the virus and its host, eight digital gene expression libraries were examined in a Bm5 cell line before infection and at 1.5, 3, 6, 12, 24, 48, and 96 h postinfection. Gene set enrichment analysis of differentially expressed genes at each time point following infection showed that gene sets including cytoskeleton, transcription, translation, energy metabolism, iron ion metabolism, and the ubiquitin-proteasome pathway were altered after viral infection. In addition, a time course depicting protein-protein interaction networks between the baculovirus and the host were constructed and revealed that viral proteins interact with a multitude of cellular machineries, such as the proteasome, cytoskeleton, and spliceosome. Several viral proteins, including IE2, CG30, PE38, and PK-1/2, were predicted to play key roles in mediating virus-host interactions. Based on these results, we tested the role of the ubiquitin-proteasome pathway and iron ion metabolism in the viral infection cycle. Treatment with a proteasome inhibitor and deferoxamine mesylate in vitro and in vivo confirmed that these pathways regulate viral infection. Taken together, these findings provide new insights into the interaction between the baculovirus and its host and identify molecular mechanisms that can be used to block viral infection and improve baculovirus expression systems.

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Section: Discussionsupporting

confidence: 46%

Section: Discussionmentioning

confidence: 86%

Dynamic Interactions between Bombyx mori Nucleopolyhedrovirus and Its Host Cells Revealed by Transcriptome Analysis

Xue

Qiao

Zhang

et al. 2012

J Virol

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“…There are also reports of insect viruses causing cell cycle arrest, including Autographa californica nucleopolyhedrovirus (AcMNPV) (a large DNA virus of the family Baculoviridae ) which arrests Sf9 insect cells in the G2/M phase [49]. Similarly, Helicoverpa armigera single-nucelocapsid nucleopolyhedrovirus (HaSNPV), causes a G2/M phase arrest in Hz-AM1 cells due to an accumulation of cyclin B1, in a manner reminiscent of parvoviruses [50]. …”

Section: Discussionmentioning

confidence: 99%

Bluetongue virus infection induces aberrant mitosis in mammalian cells

Shaw

Brüning-Richardson

Morrison

et al. 2013

Virol J

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BackgroundBluetongue virus (BTV) is an arbovirus that is responsible for ‘bluetongue’, an economically important disease of livestock. Although BTV is well characterised at the protein level, less is known regarding its interaction with host cells. During studies of virus inclusion body formation we observed what appeared to be a large proportion of cells in mitosis. Although the modulation of the cell cycle is well established for many viruses, this was a novel observation for BTV. We therefore undertook a study to reveal in more depth the impact of BTV upon cell division.MethodsWe used a confocal microscopy approach to investigate the localisation of BTV proteins in a cellular context with their respective position relative to cellular proteins. In addition, to quantitatively assess the frequency of aberrant mitosis induction by the viral non-structural protein (NS) 2 we utilised live cell imaging to monitor HeLa-mCherry tubulin cells transfected with a plasmid expressing NS2.ResultsOur data showed that these ‘aberrant mitoses’ can be induced in multiple cell types and by different strains of BTV. Further study confirmed multiplication of the centrosomes, each resulting in a separate mitotic spindle during mitosis. Interestingly, the BTV NS1 protein was strongly localised to the centrosomal regions. In a separate, yet related observation, the BTV NS2 protein was co-localised with the condensed chromosomes to a region suggestive of the kinetochore. Live cell imaging revealed that expression of an EGFP-NS2 fusion protein in HeLa-mCherry tubulin cells also results in mitotic defects.ConclusionsWe hypothesise that NS2 is a microtubule cargo protein that may inadvertently disrupt the interaction of microtubule tips with the kinetochores during mitosis. Furthermore, the BTV NS1 protein was distinctly localised to a region encompassing the centrosome and may therefore be, at least in part, responsible for the disruption of the centrosome as observed in BTV infected mammalian cells.

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“…Three PIFs have previously been determined to play a role in the specific binding of ODV to midgut cells. P74 has been shown to function as an attachment protein and to bind to a 30-kDa host receptor protein on primary target cells within the midgut (17,40). PIF-1 and PIF-2 also mediate the specific binding of ODV to midgut target cells (28).…”

Section: Discussionmentioning

confidence: 99%

Autographa californica Multiple Nucleopolyhedrovirus Core Gene ac96 Encodes a Per Os Infectivity Factor ( pif-4 )

Mao

Nie

Harris

et al. 2009

J Virol

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Autographa californica multiple nucleopolyhedrovirus (AcMNPV) ac96 is a core gene, but its role in virus replication is still unknown. To determine its role in the baculovirus life cycle, we used the AcMNPV bacmid system to generate an ac96-null virus (vAc 96null ). Our analyses showed that the absence of ac96 does not affect budded virus (BV) production or viral DNA replication in infected Sf9 cells. Western blotting and confocal immunofluorescence analysis showed that AC96 is expressed in both the cytoplasm and the nucleus throughout infection. In addition, AC96 was detected in the envelope fractions of both BV and occlusion-derived virus. Injection of vAc96null BV into the hemocoel killed Trichoplusia ni larvae as efficiently as repaired and control viruses; however, vAc 96null was unable to infect the midgut tissue of Trichoplusia ni larvae when inoculated per os. Therefore, the results of this study show that ac96 encodes a new per os infectivity factor (PIF-4).

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Heliocoverpa armigera single nucleocapsid nucleopolyhedrovirus induces Hz-AM1 cell cycle arrest at the G2 phase with accumulation of cyclin B1

Cited by 13 publications

References 25 publications

Dynamic Interactions between Bombyx mori Nucleopolyhedrovirus and Its Host Cells Revealed by Transcriptome Analysis

Dynamic Interactions between Bombyx mori Nucleopolyhedrovirus and Its Host Cells Revealed by Transcriptome Analysis

Bluetongue virus infection induces aberrant mitosis in mammalian cells

Autographa californica Multiple Nucleopolyhedrovirus Core Gene ac96 Encodes a Per Os Infectivity Factor ( pif-4 )

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