ArticleArchives of virology2025
Proteomic analysis identifies intracellular targets for avian coronavirus NSP10.
Article in Archives of virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- IRES Mutation Confers a Replicative Advantage to SVA by Enhancing Translation Efficiency.Transboundary and emerging diseases · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Avian coronavirus, also known as infectious bronchitis virus (IBV), is the causative agent of infectious bronchitis (IB). The non-structural proteins (NSPs) of IBV are critical for viral replication and for evading the host's immune response. The innate immune response serves as the first line of defense against viral infections. The IBV genome codes for 15 NSPs (NSP2-16). In this study, we identified host proteins interacting with IBV NSP10 using co-immunoprecipitation (Co-IP) and liquid chromatography-tandem mass spectrometry (LC/MS/MS). Proteomic analysis revealed that interactions of host proteins with NSP10 are involved in processes such as localization, transport, and metabolism, regulation of the cell cycle, and antiviral responses. We further explored the role of NSP10 in these immune and cellular regulation pathways and also confirmed the interaction between NSP10 and the host protein hnRNPA1. Further investigation showed that hnRNPA1 inhibited IBV replication. It is speculated that the binding of hnRNP A1 to NSP10 interferes with the function of the replication complex, thereby inhibiting virus replication. However, co-overexpression of NSP10 and hnRNP A1 partially restored viral replication, suggesting a complex relationship between these two proteins. These findings demonstrate that IBV NSP10 plays a significant role in viral infection and in modulating host cell processes, highlighting its potential as a target for therapeutic interventions.
Indexed as
Identifiers
40080214What OpenQuestion holds
Registered trials
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.