ArticleVirus genes2015
Identification of NS1 domains of avian H5N1 influenza virus which influence the interaction with the NOLC1 protein.
Article in Virus genes, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- The H5N1-NS1 protein affects the host cell cycle and apoptosis through interaction with the host lncRNA PIK3CD-AS2.Virus genes · 2025Article
- Article
- Roles of NOLC1 in cancers and viral infection.Journal of cancer research and clinical oncology · 2023Review
- Interaction of influenza A virus NS1 and cytoskeleton scaffolding protein α-actinin 4.Virus genes · 2022Article
- Species-Specific Host-Virus Interactions: Implications for Viral Host Range and Virulence.Trends in microbiology · 2020Review
- The interaction between NOLC1 and IAV NS1 protein promotes host cell apoptosis and reduces virus replication.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-structural protein 1 (NS1) is an important virulence factor encoded by influenza A virus. NS1 can interact with a variety of host cell proteins to interfere with the host innate immune response and to promote effective viral replication. Our previous work has shown that only the effector domain of NS1 (amino acid residues 74-230/237) is sufficient to interact with nucleolar and coiled-body phosphoprotein 1 (NOLC1). To investigate the exact region of NS1 that interacts with NOLC1, we used only the effector domain of NS1 and constructed various mutants having different deletions, and then tested their ability to interact with NOLC1 via pull-down assay. Only the mutant containing amino acid residues 104-200 showed positive interaction with NOLC1. To further determine the key amino acids of the NS1 effector domain which are crucial for interaction with NOLC1, several mutants containing a single amino acid substitution were made and their interaction with NOLC1 was tested. Only the mutant D120A or R195A showed reduced binding with NOLC1, suggesting that D120 and R195 were crucial to the binding of NS1 to NOLC1. This study lays the foundation for further research aiming at furthering our understanding of the interaction between NS1 and host cells.
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