ArticleBMC veterinary research2025
The nonstructural protein 13 of porcine deltacoronavirus coordinates ATP-driven duplex unwinding and ATP-independent strand annealing for nucleic acid remodeling.
Article in BMC veterinary research, 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.
- Porcine Deltacoronavirus Nsp13 Suppresses the Assembly of the MAVS-TBK1-IRF3 Complex and IRF9 Nuclear Translocation.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
5 authors.
Funding
Abstract
backgroundSwine diarrheal death caused by intestinal coronavirus is a key problem that needs to be solved urgently in pig production. Porcine deltacoronavirus (PDCoV) is a novel enteropathogenic coronavirus that causes acute diarrhea in suckling piglets, resulting in serious economic losses to the cultivation industry. PDCoV helicase NSP13 plays a pivotal role in virus replication and is regarded as an ideal drug target, but its enzymatic characteristics remain poorly characterized.
resultsIn this study, we systematically investigated the biochemical properties of PDCoV NSP13 through recombinant expression and functional assays. Our findings revealed that PDCoV NSP13 exhibited a 5'-to-3' directional unwinding activity powered by broad-spectrum nucleoside triphosphate hydrolysis, with the enhanced unwinding efficiency for dsDNA over dsRNA. Furthermore, we found that 4 nt was the minimum length of 5'-overhang required for NSP13 to unwind substrates, and the unwinding efficiency was inversely correlated with both 5'-overhang length and duplex region size. And NSP13 displayed concentration-dependent activity modulation, whereas excess NSP13 levels suppressed the unwinding reaction. Notably, we uncovered a previously unrecognized strand-annealing capability of NSP13, enabling efficient hybridization of complementary ssDNA into dsDNA. And a series of experiments with protein mutants revealed the effect of deletion of different domains on the unwinding and annealing activities of PDCoV NSP13.
conclusionsThese mechanistic insights advanced our understanding of coronavirus replication machinery and established a biochemical foundation for the development of antiviral drugs targeting helicase NSP13.
Indexed as
Identifiers
What 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.