Seneca Valley virus attachment and uncoating mediated by its receptor anthrax toxin receptor 1

Cao, Lin; Zhang, Ran; Liu, Tingting; Sun, Zhenli; Hu, M.H.; Sun, Yuna; Cheng, Lingpeng; Guo, Yu; Fu, Sheng; Hu, Junjie; Li, Xiangmin; Yu, Changjun; Wang, Hanyang; Chen, Huanchun; Li, Xueming; Fry, Elizabeth E.; Stuart, D.I.; Qian, Ping; Lou, Zhiyong; Rao, Zihe

doi:10.1073/pnas.1814309115

Cited by 32 publications

(28 citation statements)

References 49 publications

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“…Culture supernatants were harvested and re-inoculated onto fresh BHK-21 cells until the typical CPE of SVV appeared. The virus was purified by CsCl-gradient ultracentrifugation (1.33 g /ml) (Seshidhar et al, 2007; Cao et al, 2018).…”

Section: Methodsmentioning

confidence: 99%

Seneca Valley Virus 2C and 3Cpro Induce Apoptosis via Mitochondrion-Mediated Intrinsic Pathway

Liu

et al. 2019

Front. Microbiol.

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Seneca Valley virus (SVV) is the only member of the genus Senecavirus of the Picornaviridae family. SVV can selectively infect and lyse tumor cells with neuroendocrine features and is used as an oncolytic virus for treating small-cell lung cancers. However, the detailed mechanism underlying SVV-mediated destruction of tumor cells remains unclear. In this study, we found that SVV can increase the proportion of apoptotic 293T cells in a dose- and time-dependent manner. SVV-induced apoptosis was initiated via extrinsic and intrinsic pathways through activation of caspase-3, the activity of which could be attenuated by a pan-caspase inhibitor (Z-VAD-FMK). We confirmed that SVV 2C and 3C pro play critical roles in SVV-induced apoptosis. The SVV 2C protein was located solely in the mitochondria and activated caspase-3 to induce apoptosis. SVV 3C pro induced apoptosis through its protease activity, which was accompanied by release of cytochrome C into the cytoplasm, but did not directly cleave PARP1.

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Section: Methodsmentioning

confidence: 99%

Seneca Valley Virus 2C and 3Cpro Induce Apoptosis via Mitochondrion-Mediated Intrinsic Pathway

Liu

et al. 2019

Front. Microbiol.

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“…Not only is the Nluc smaller ( ~500 nt) than either firefly or Renilla luciferase, it is also more stable to environmental conditions as well as produces brighter and more sustained luminescence (Hall et al 2012 ). In the cases of Nluc-expressing flaviviruses, the enzyme activity was quantified in a simple manner or a high-throughput assay to assess the antiviral activity of potential inhibitors in vitro (Cao et al 2018 ; Pierson et al 2017 ). The brilliantly red fluorescent protein TagRFP (RFP) is derived from Entacmaea quadricolor with a size of ~ 700 nt comparable to the one of GFP (Subach et al 2008 ).…”

Section: Discussionmentioning

confidence: 99%

“…ANTXR1, also known as tumor endothelial marker 8 (TEM8), was first identified as the cell surface receptor of anthrax toxin (Miles et al 2017 ). Unlike ANTXR2, another anthrax toxin receptor with a wide distribution in the adult tissues, ANTXR1, is abundant in the tumor cells and the vasculature of developing embryos (Cao et al 2018 ; Chaudhary et al 2012 ). Among 1037 cell lines in the Cancer Cell Line Encyclopedia, over 63% of cell lines exceed the expression cutoff of ANTXR1 (Miles et al 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Infectious recombinant Senecavirus A expressing novel reporter proteins

Wang

Mou

Chen

et al. 2021

Appl Microbiol Biotechnol

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Senecavirus A (SVA) is an emerging picornavirus that has been associated with vesicular disease and neonatal mortality in swine. The construction of SVA virus carrying foreign reporter gene provides a powerful tool in virus research. However, it is often fraught with rescuing a recombinant picornavirus harboring a foreign gene or maintaining the stability of foreign gene in the virus genome. Here, we successfully generated recombinant SVA GD05/2017 viruses (V-GD05-clone) expressing the green fluorescent protein (iLOV), red fluorescent protein (RFP), or NanoLuc luciferase (Nluc). These recombinant viruses have comparable growth kinetics to the parental virus. Genetic stability analysis indicated that V-GD05-iLOV was highly stable in retaining iLOV gene for more than 10 passages, while V-GD05-RFP and V-GD05-Nluc lost the foreign genes in five passages. In addition, high-intensity fluorescent signals were found in the V-GD05-RFP- and V-GD05-iLOV-infected cells by fluorescence observation and flow cytometry analysis, and the luciferase activity assay could quantitatively monitor the replication of V-GD05-Nluc. In order to identify the porcine cell receptor for SVA, anthrax toxin receptor 1 (ANTXR1) was knocked out or overexpressed in the ST-R cells. The ANTXR1 knock-out cells lost the ability for SVA infection, while overexpression of ANTXR1 significantly increased the cell permissivity. These results confirmed that ANTXR1 was the receptor for SVA to invade porcine cells as reported in the human cells. Overall, this study suggests that these SVA reporter viruses will be useful tools in elucidating virus pathogenesis and developing control measures. Key points • We successfully generated SVA viruses expressing the iLOV, RFP, or Nluc. • The iLOV was genetically stable in the V-GD05-iLOV genome over ten passages. • ANTXR1 was the receptor for SVA to invade porcine cells. Supplementary Information The online version contains supplementary material available at 10.1007/s00253-021-11181-6.

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“…Most of the hotspots identified at the interpentamer interfaces in this study were conserved with residues in other picornaviruses that were previously predicted to stabilize the capsid. For example, hotspots N25, R61, Y62, Y63, T64, V95, R102, N117, S240 (VP2), M144, Y148, I150, D152, L153, T194 and T197 (VP3) correspond to residues in Seneca Valley virus 1 (SVV-1) that were proposed to form stabilizing interactions across the pentamer-pentamer interface [54], while hotspot residues R61, T64, (VP2), M144 and D152 (VP3) were conserved with residues that were predicted to be important for the stability of the pentamer interfaces of enteroviruses [36]. Furthermore, hotspots M144, I150, D152 and L153 (VP3) are conserved with residues in human rhinovirus (HRV)-2 that become disordered during uncoating and RNA release [56].…”

Section: Discussionmentioning

confidence: 99%

The In Silico Prediction of Hotspot Residues that Contribute to the Structural Stability of Subunit Interfaces of a Picornavirus Capsid

Upfold

Ross

Bishop

et al. 2020

Viruses

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The assembly of picornavirus capsids proceeds through the stepwise oligomerization of capsid protein subunits and depends on interactions between critical residues known as hotspots. Few studies have described the identification of hotspot residues at the protein subunit interfaces of the picornavirus capsid, some of which could represent novel drug targets. Using a combination of accessible web servers for hotspot prediction, we performed a comprehensive bioinformatic analysis of the hotspot residues at the intraprotomer, interprotomer and interpentamer interfaces of the Theiler’s murine encephalomyelitis virus (TMEV) capsid. Significantly, many of the predicted hotspot residues were found to be conserved in representative viruses from different genera, suggesting that the molecular determinants of capsid assembly are conserved across the family. The analysis presented here can be applied to any icosahedral structure and provides a platform for in vitro mutagenesis studies to further investigate the significance of these hotspots in critical stages of the virus life cycle with a view to identify potential targets for antiviral drug design.

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Seneca Valley virus attachment and uncoating mediated by its receptor anthrax toxin receptor 1

Cited by 32 publications

References 49 publications

Seneca Valley Virus 2C and 3Cpro Induce Apoptosis via Mitochondrion-Mediated Intrinsic Pathway

Seneca Valley Virus 2C and 3Cpro Induce Apoptosis via Mitochondrion-Mediated Intrinsic Pathway

Infectious recombinant Senecavirus A expressing novel reporter proteins

The In Silico Prediction of Hotspot Residues that Contribute to the Structural Stability of Subunit Interfaces of a Picornavirus Capsid

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