Voltage-Dependent Anion Channel 1 Interacts with Ribonucleoprotein Complexes To Enhance Infectious Bursal Disease Virus Polymerase Activity

Han, Chunyan; Zeng, Xianying; Yao, Shuai; Gao, Li; Zhang, Lizhou; Qi, Xiaole; Duan, Yulu; Yang, Bo; Gao, Yulong; Liu, Changjun; Zhang, Yanping; Wang, Yongqiang; Wang, Xiaomei

doi:10.1128/jvi.00584-17

Cited by 28 publications

(21 citation statements)

References 43 publications

(48 reference statements)

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“…Combining the protein functional analysis in the current study with previous reports (Dumas et al, 2015;Jovasevic et al, 2015;Han et al, 2017), we also observed that MAPRE1 and VDAC1 were related to virus infection. MAPRE1, also known as endbinding protein 1 (EB1), acts as a master regulator of plus-end tracking proteins (+TIPs) networks by targeting the growing ends of microtubules and recruiting other + TIPs and finally regulates the microtubule dynamics (Galjart, 2010).…”

Section: Discussionsupporting

confidence: 82%

“…VDAC1 was also involved in the infection of viruses, such as infectious bursal disease virus (IBDV). VDAC1 could interact with IBDV Ribonucleoprotein (RNPs) and facilitates IBDV replication by enhancing IBDV polymerase activity (Han et al, 2017). In our previous work, we have confirmed that CSFV infection was closely associated with mitochondrial function (Gou et al, 2017;Ma et al, 2019).…”

Section: Discussionmentioning

confidence: 60%

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The Network of Interactions Between Classical Swine Fever Virus Nonstructural Protein p7 and Host Proteins

et al. 2020

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Classical swine fever (CSF) is a highly contagious viral disease causing severe economic losses to the swine industry. As viroporins of viruses modulate the cellular ion balance and then take over the cellular machinery, blocking the activity of viroporin or developing viroporin-defective attenuated vaccines offers new approaches to treat or prevent viral infection. Non-structural protein p7 of CSF virus (CSFV) is a viroporin, which was highly involved in CSFV virulence. Deciphering the interaction between p7 and host proteins will aid our understanding of the mechanism of p7-cellular protein interaction affecting CSFV replication. In the present study, seven host cellular proteins including microtubule-associated protein RP/EB family member 1 (MAPRE1), voltage-dependent anion channel 1 (VDAC1), proteasome maturation protein (POMP), protein inhibitor of activated STAT 1 (PIAS1), gametogenetin binding protein 2 (GGNBP2), COP9 signalosome subunit 2 (COPS2), and contactin 1 (CNTN1) were identified as the potential interactive cellular proteins of CSFV p7 by using yeast two-hybrid (Y2H) screening. Plus, the interaction of CSFV p7 with MAPRE1 and VDAC1 was further evaluated by co-immunoprecipitation and GST-pulldown assay. Besides, the p7-cellular protein interaction network was constructed based on these seven host cellular proteins and the STRING database. Enrichment analysis of GO and KEGG indicated that many host proteins in the p7-cellular protein interaction network were mainly related to the ubiquitin-proteasome system, cGMP-PKG signaling pathway, calcium signaling pathway, and JAK-STAT pathway. Overall, this study identified potential interactive cellular proteins of CSFV p7, constructed the p7-cellular protein interaction network, and predicted the potential pathways involved in the interaction between CSFV p7 and host cells.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 60%

The Network of Interactions Between Classical Swine Fever Virus Nonstructural Protein p7 and Host Proteins

et al. 2020

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“…Gef1p Cl - silencing, a homologue of the mammalian CLC proteins in yeast, inhibited replication through its downstream effects on Cu 2+ homoeostasis, inhibiting the functionality of the viral replicase. Direct interaction of the voltage-dependent anion channel 1 with VP1 and VP3 of infectious bursal disease virus (family Birnavirdae ) was shown to stabilize the ribonucleoprotein complex, allowing full activity of the viral polymerase [38]. It may be possible that CLIC1, as an nsP3 interacting protein, is required for CHIKV genome replication for a similar mechanism.…”

Section: Discussionmentioning

confidence: 99%

Chikungunya virus requires cellular chloride channels for efficient genome replication

et al. 2019

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Chikungunya virus (CHIKV) is a re-emerging, pathogenic alphavirus that is transmitted to humans by Aedes spp. mosquitoes—causing fever and debilitating joint pain, with frequent long-term health implications and high morbidity. The CHIKV lifecycle is poorly understood and specific antiviral therapeutics or vaccines are lacking. In this study, we investigated the role of host-cell chloride (Cl-) channels on CHIKV replication.We demonstrate that specific pharmacological Cl- channel inhibitors significantly inhibit CHIKV replication in a dose-dependent manner, suggesting that Cl-channels are pro-viral factors in human cells. Further analysis of the effect of the inhibitors on CHIKV attachment, entry, viral protein expression and replicon replication demonstrated that Cl- channels are specifically required for efficient CHIKV genome replication. This was conserved in mosquito cells, where CHIKV replication and genome copy number was significantly reduced following Cl- channel inhibition. siRNA silencing identified chloride intracellular channels 1 and 4 (CLIC1 and CLIC4, respectively) as required for efficient CHIKV replication and protein affinity chromatography showed low levels of CLIC1 in complex with CHIKV nsP3, an essential component of the viral replication machinery. In summary, for the first time we demonstrate that efficient replication of the CHIKV genome depends on cellular Cl- channels, in both human and mosquito cells and identifies CLIC1 and CLIC4 as agonists of CHIKV replication in human cells. We observe a modest interaction, either direct or indirect, between CLIC1 and nsP3 and hypothesize that CLIC1 may play a role in the formation/maintenance of CHIKV replication complexes. These findings advance our molecular understanding of CHIKV replication and identify potential druggable targets for the treatment and prevention of CHIKV mediated disease.

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“…Han et al showed that knockdown of VDAC1 inhibited IBDV replication through the reduction of viral polymerase activity, and that the overexpression of VDAC1 promotes polymerase activity. Immunoprecipitation (IP) experiments showed that VDAC1 interacts with IBDV VP1 and VP3, components of RNPs, indicating a role for this channel in RNP formation [64].…”

Section: − Channels or Other Anions And Vials Replicationmentioning

confidence: 99%

Ion Channels as Therapeutic Targets for Viral Infections: Further Discoveries and Future Perspectives

Charlton

Pearson

Hover

et al. 2020

Viruses

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Ion channels play key roles in almost all facets of cellular physiology and have emerged as key host cell factors for a multitude of viral infections. A catalogue of ion channel-blocking drugs have been shown to possess antiviral activity, some of which are in widespread human usage for ion channel-related diseases, highlighting new potential for drug repurposing. The emergence of ion channel–virus interactions has also revealed the intriguing possibility that channelopathies may explain some commonly observed virus induced pathologies. This field is rapidly evolving and an up-to-date summary of new discoveries can inform future perspectives. We herein discuss the role of ion channels during viral lifecycles, describe the recently identified ion channel drugs that can inhibit viral infections, and highlight the potential contribution of ion channels to virus-mediated disease.

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Voltage-Dependent Anion Channel 1 Interacts with Ribonucleoprotein Complexes To Enhance Infectious Bursal Disease Virus Polymerase Activity

Cited by 28 publications

References 43 publications

The Network of Interactions Between Classical Swine Fever Virus Nonstructural Protein p7 and Host Proteins

The Network of Interactions Between Classical Swine Fever Virus Nonstructural Protein p7 and Host Proteins

Chikungunya virus requires cellular chloride channels for efficient genome replication

Ion Channels as Therapeutic Targets for Viral Infections: Further Discoveries and Future Perspectives

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