Abstract
NS1 protein is the only non-structural protein encoded by the influenza A virus, and it contributes significantly to disease pathogenesis by modulating many virus and host cell processes. A two-hybrid screen for proteins that interact with NS1 from influenza A yielded growth arrest-specific protein 8. Gas8 associated with NS1 in vitro and in vivo. Deletion analysis revealed that the N-terminal 260 amino acids of Gas8 were able to interact with NS1, and neither the RNA-binding domain nor the effector domain of NS1 was sufficient for the NS1 interaction. We also found that actin, myosin, and drebrin interact with Gas8. NS1 and β-actin proteins could be co-immunoprecipitated from extracts of transfected cells. Furthermore, actin and Gas8 co-localized at the plasma membrane. These results are discussed in relation to the possible functions of Gas8 protein and their relevance in influenza virus release.
Highlights
Influenza A viral NS1 protein is a multifunctional protein that is capable of both protein-protein and protein-RNA interactions [1]
Cells and cell culture 293FT, Hela, CV-1, NIH3T3, and BHK21 cells were maintained in Dulbecco's Modified Eagle's Medium (DMEM) containing 10% heat-inactivated fetal calf serum (HyClone)
Construction of plasmids To generate the NS1 expression construct for the CytoTrap two-hybrid system, cDNAs encoding the NS1 proteins of A/Swine/Colorado/1/77 (H3N2) were amplified using the primers listed in Table 1 and cloned into pSos, creating pSos-NS1
Summary
Influenza A viral NS1 protein is a multifunctional protein that is capable of both protein-protein and protein-RNA interactions [1]. It binds non- to doublestranded RNA and to protein targets. NS1 binds directly to p85β to activate phosphatidylinositol 3kinase signaling [2]. It binds a cleavage and polyadenylation specificity factor to inhibit the maturation and export of host antiviral mRNAs, and it inhibits poly(A)-binding protein II [3]. Association of NS1 protein with host factors may affect apoptosis [10,11]
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