Abstract
BackgroundDuring the process that AIV infect hosts, the NS1 protein can act on hosts, change corresponding signal pathways, promote the translation of virus proteins and result in virus replication.ResultsIn our study, we found that PARP domain and Glu-rich region of PARP10 interacted with NS1, and the presence of NS1 could induce PARP10 migrate from cytoplasm to nucleus. NS1 high expression could reduce the endogenous PARP10 expression. Cell cycle analysis showed that with inhibited PARP10 expression, NS1 could induce cell arrest in G2-M stage, and the percentage of cells in G2-M stage rise from the previous 10%-45%, consistent with the cell proliferation result. Plague forming unit measurement showed that inhibited PARP10 expression could help virus replication.ConclusionsIn a word, our results showed that NS1 acts on host cells and PARP10 plays a regulating role in virus replication.
Highlights
During the process that avian influenza virus (AIV) infect hosts, the NS1 protein can act on hosts, change corresponding signal pathways, promote the translation of virus proteins and result in virus replication
NS1 interacts with poly (ADP-ribose) polymerases 10 (PARP10) To verify the screening result of yeast two-hybrid system, we identified the in vivo and in vitro interaction between NS1 and PARP10
The sediment was examined by Western blotting using anti-Myc antibody, and the result showed that GST-NS1 could bind and sediment PARP10, while GST could not (Figure 1a), indicating that NS1 protein in vitro could interact with PARP10
Summary
During the process that AIV infect hosts, the NS1 protein can act on hosts, change corresponding signal pathways, promote the translation of virus proteins and result in virus replication. The NS1 protein of avian influenza virus (AIV) is present in host cells infected by the virus instead of being present in mature virions, so it is called nonstructural protein (NS) [1]. The NS1 protein has two nuclear localization signals, which can induce synthesized NS1 migrate rapidly to nuclei, and aggregate in nuclei early infected by virus. Studies show that amino-terminal RNA binding region and carboxyl-terminal effector domain of the NS1 protein are closely related to protein synthesis in host cells [3,4]. Effector domain of the NS1 protein can interact with nuclear protein of host
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