The PA-interacting host protein nucleolin acts as an antiviral factor during highly pathogenic H5N1 avian influenza virus infection

Zhao, Guimin; Hu, Jiao; Wang, Xiaoquan; Yang, Qian; Liang, Yanyan; Ma, Cuiqing; Liu, Dong; Liu, Kaituo; Hao, Xiaoli; Gu, Minghong; Liu, Xiaowen; Jiao, Xinan

doi:10.1007/s00705-018-3926-3

Cited by 12 publications

(14 citation statements)

References 58 publications

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“…These studies are all examples of how nucleolins can positively promote virus growth, and some studies have shown that nucleolins can inhibit virus growth. For example, NCL is identified as a potential antiviral host factor that inhibits influenza A virus (IAV) replication [ 38 ]. In our study, we also demonstrated that NCL not only interacts with PPRV N protein, but also plays a negative regulatory role in PPRV growth.…”

Section: Discussionmentioning

confidence: 99%

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Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Dong

Zhu

Miao

et al. 2020

Journal of General Virology

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Peste des petits ruminants (PPR) is a highly contagious disease of small ruminants that is caused by peste des petits ruminants virus (PPRV). To date, the molecular mechanism of PPRV infection is still unclear. It is well known that host proteins might be involved in the pathogenesis process for many viruses. In this study, we first proved that nucleolin (NCL), a highly conserved host factor, interacts with the core domain of PPRV N protein through its C terminus and co-locates with the N protein in the nucleus of cells. To investigate the role of NCL in PPRV infection, the expression level of NCL was inhibited with small interfering RNAs of NCL, and the results showed that PPRV growth was improved. However, the proliferation of PPRV was inhibited when the expression level of NCL was improved. Further analysis indicated that the inhibitory effect of NCL on the PPRV was caused by stimulating the interferon (IFN) pathways in host cells. In summary, our results will help us to understand the mechanism of PPRV infection.

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Section: Discussionmentioning

confidence: 99%

“…Likewise, NCL silences human immunodeficiency virus (HIV)-1 transcription by stabilizing G-quadruplex structures folded by the long terminal repeat promoter [ 37 ]. Furthermore, NCL has been proved to act as a novel potential antiviral factor during H5N1 infection [ 38 ].…”

Section: Introductionmentioning

confidence: 99%

Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Dong

Zhu

Miao

et al. 2020

Journal of General Virology

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“…Preliminary experiments suggest that PARP1 was pulled down by NP in the presence of viral RNA, but associated most strongly with RdRP complexes containing NP but treated with RNase to remove viral RNA (Figures S3). We observed that NPM, a binding partner of another polymerase interactor NCL [56], could also effectively displace PARP1 from interaction with NP. It could be that RNA organizes the NP and polymerase proteins in a manner that is refractory to interaction with PARP1 (Figures S3A and S3C).…”

Section: Discussionmentioning

confidence: 99%

Poly-ADP Ribosyl Polymerase 1 (PARP1) Regulates Influenza A Virus Polymerase

Westera

Jennings

Maamary

et al. 2019

Advances in Virology

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Influenza A viruses (IAV) are evolutionarily successful pathogens, capable of infecting a number of avian and mammalian species and responsible for pandemic and seasonal epidemic disease in humans. To infect new species, IAV typically must overcome a number of species barriers to entry, replication, and egress, even while virus replication is counteracted by antiviral host factors and innate immune mechanisms. A number of host factors have been found to regulate the replication of IAV by interacting with the viral RNA-dependent RNA polymerase (RdRP). The host factor PARP1, a poly-ADP ribosyl polymerase, was required for optimal functions of human, swine, and avian influenza RdRP in human 293T cells. In IAV infection, PARP1 was required for efficient synthesis of viral nucleoprotein (NP) in human lung A549 cells. Intriguingly, pharmacological inhibition of PARP1 enzymatic activity (PARylation) by 4-amino-1,8-naphthalimide led to a 4-fold increase in RdRP activity, and a 2.3-fold increase in virus titer. Exogenous expression of the natural PARylation inhibitor PARG also enhanced RdRP activity. These data suggest a virus-host interaction dynamic where PARP1 protein itself is required, but cellular PARylation has a distinct suppressive modality, on influenza A viral polymerase activity in human cells.

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“…Another group showed nucleolin (NCL), a novel PA-interacting host protein, significantly decreased IAV replication in the case of H5N1 infection in HEK293T cells by decreasing inflammatory responses. The antiviral mechanisms of NCL may pave the way to develop new anti-influenza drugs [303].…”

Section: Referencementioning

confidence: 99%

The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections

Mehrbod¹,

et al. 2019

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Virus infection induces different cellular responses in infected cells. These include cellular stress responses like autophagy and unfolded protein response (UPR). Both autophagy and UPR are connected to programed cell death I (apoptosis) in chronic stress conditions to regulate cellular homeostasis via Bcl2 family proteins, CHOP and Beclin-1. In this review article we first briefly discuss arboviruses, influenza virus, and HIV and then describe the concepts of apoptosis, autophagy, and UPR. Finally, we focus upon how apoptosis, autophagy, and UPR are involved in the regulation of cellular responses to arboviruses, influenza virus and HIV infections.

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The PA-interacting host protein nucleolin acts as an antiviral factor during highly pathogenic H5N1 avian influenza virus infection

Cited by 12 publications

References 58 publications

Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Nucleolin (NCL) inhibits the growth of peste des petits ruminants virus

Poly-ADP Ribosyl Polymerase 1 (PARP1) Regulates Influenza A Virus Polymerase

The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections

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