ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 59 citations in OpenAlex.
- Repurposed clindamycin suppresses pyroptosis in tumor-associated macrophages through Inhibition of caspase-1.Journal of experimental & clinical cancer research : CR · 2025Article
- Site-selective photo-crosslinking for the characterisation of transient ubiquitin-like protein-protein interactions.PloS one · 2025Article
- Natural History of Influenza B Virus-Current Knowledge on Treatment, Resistance and Therapeutic Options.Current issues in molecular biology · 2023Review
- Insights into the ISG15 transfer cascade by the UBE1L activating enzyme.Nature communications · 2023Article
- Existing Evidence for Influenza B Virus Adaptations to Drive Replication in Humans as the Primary Host.Viruses · 2023Review
- Article
- The Influenza B Virus Victoria and Yamagata Lineages Display Distinct Cell Tropism and Infection Induced Host Gene Expression in Human Nasal Epithelial Cell Cultures.bioRxiv : the preprint server for biology · 2023Article
- Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin.Nature communications · 2023Article
- Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin.bioRxiv : the preprint server for biology · 2023Article
- ISG15 conjugation to proteins on nascent DNA mitigates DNA replication stress.Nature communications · 2022Article
- [The Victoria and Yamagata Lineages of Influenza B Viruses, unknown and undervalued].Revista espanola de quimioterapia : publicacion oficial de la Sociedad Espanola de Quimioterapia · 2022Review
- Review
- Modulation of Extracellular ISG15 Signaling by Pathogens and Viral Effector Proteins.Cell reports · 2020Article
- Robust induction of interferon and interferon-stimulated gene expression by influenza B/Yamagata lineage virus infection of A549 cells.PloS one · 2020Article
- Lianhua-Qingwen Displays Antiviral and Anti-Inflammatory Activity and Synergistic Effects with Oseltamivir against Influenza B Virus Infection in the Mouse Model.Evidence-based complementary and alternative medicine : eCAM · 2020Article
- The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection.Nature communications · 2019Article
- ISG15: It's Complicated.Journal of molecular biology · 2019Review
- Structural insights into the species preference of the influenza B virus NS1 protein in ISG15 binding.Protein & cell · 2019Article
- Article
- Structure of interferon-stimulated gene product 15 (ISG15) from the bat species Myotis davidii and the impact of interdomain ISG15 interactions on viral protein engagement.Acta crystallographica. Section D, Structural biology · 2019Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Interferon-induced ISG15 conjugation plays an important antiviral role against several viruses, including influenza viruses. The NS1 protein of influenza B virus (NS1B) specifically binds only human and nonhuman primate ISG15s and inhibits their conjugation. To elucidate the structural basis for the sequence-specific recognition of human ISG15, we determined the crystal structure of the complex formed between human ISG15 and the N-terminal region of NS1B (NS1B-NTR). The NS1B-NTR homodimer interacts with two ISG15 molecules in the crystal and also in solution. The two ISG15-binding sites on the NS1B-NTR dimer are composed of residues from both chains, namely residues in the RNA-binding domain (RBD) from one chain, and residues in the linker between the RBD and the effector domain from the other chain. The primary contact region of NS1B-NTR on ISG15 is composed of residues at the junction of the N-terminal ubiquitin-like (Ubl) domain and the short linker region between the two Ubl domains, explaining why the sequence of the short linker in human and nonhuman primate ISG15s is essential for the species-specific binding of these ISG15s. In addition, the crystal structure identifies NS1B-NTR binding sites in the N-terminal Ubl domain of ISG15, and shows that there are essentially no contacts with the C-terminal Ubl domain of ISG15. Consequently, NS1B-NTR binding to ISG15 would not occlude access of the C-terminal Ubl domain of ISG15 to its conjugating enzymes. Nonetheless, transfection assays show that NS1B-NTR binding of ISG15 is responsible for the inhibition of interferon-induced ISG15 conjugation in cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.