ArticleMicrobiology spectrum2022
Free ISG15 Inhibits the Replication of Peste des Petits Ruminants Virus by Breaking the Interaction of Nucleoprotein and Phosphoprotein.
Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 2 citations in OpenAlex.
- Modification of PCNA by ISG15 plays a crucial role in porcine deltacoronavirus infection.Veterinary research · 2026Article
- Sepsis reporting signals associated with endothelin receptor antagonists and IFITM3-Centered interferon-responsive monocyte features: a pharmacovigilance and transcriptomic study.Frontiers in pharmacology · 2026Article
- Transcriptome and proteomic analysis of mpox virus F3L-expressing cells.Frontiers in cellular and infection microbiology · 2024Article
- ISG15: its roles in SARS-CoV-2 and other viral infections.Trends in microbiology · 2023Review
- Retinoic Acid-inducible Gene-I Increases Interferon-stimulated Gene 15 Expression in Human Renal Proximal Tubule Epithelial Cells.In vivo (Athens, Greece)Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peste des petits ruminants virus (PPRV) causes a highly contagious disease in small ruminants and severe economic losses in developing countries. PPRV infection can stimulate high levels of interferon (IFN) and many IFN-stimulated genes (ISGs), such as ISG15, which may play a key role in the process of viral infection. However, the role of ISG15 in PPRV infection and replication has not yet been reported. In this study, we found ISG15 expression to be significantly upregulated after PPRV infection of caprine endometrial epithelial cells (EECs), and ISG15 inhibits the proliferation of PPRV. Further analysis showed that free ISG15 could inhibit PPRV proliferation. Moreover, ISG15 does not affect the binding, entry, and transcription but does suppress the replication of PPRV. A detailed analysis revealed that ISG15 interacts and colocalizes with both viral N and P proteins and that its interactive regions are all located in the N-terminal domain. Further studies showed that ISG15 can competitively interact with N and P proteins and significantly interfere with their binding. Finally, through the construction of the C-terminal mutants of ISG15 with different lengths, it was found that amino acids (aa) 77 to 101 play a key role in inhibiting the binding of N and P proteins and that interaction with the P protein disappears after the deletion of 77 to 101 aa. The present study revealed a novel mechanism of ISG15 in disrupting the activity of the N
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