Evidence map›Paper›PMID 40573376›Full record

ArticleViruses2025

Discovery of Small Molecules Against Foot-and-Mouth Disease Virus Replication by Targeting 2C Helicase Activity.

Saisai Zhou, Suyu Mu, Shuqi Yu, Yang Tian, Sijia Lu, Zhen Li, Hao Wu, Jiaying Zhao, Huanchun Chen, Shiqi Sun and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Viruses, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Saisai ZhouState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0009-0002-3253-0957
Suyu MuLanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.
Shuqi YuState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Yang TianState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Sijia LuState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Zhen LiState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Hao WuState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Jiaying ZhaoState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Huanchun ChenState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.
Shiqi SunLanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China.ORCID 0000-0003-4975-739X
Yunfeng SongState Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China.

Funding

National Key Research and Development Program of China 2021YFD1800303National Natural Science Foundation of China 31972658
6 · The paper itself

Abstract

backgroundThe 2C protein of foot-and-mouth disease virus (FMDV), a member of helicase superfamily 3 (SF3), drives viral genome replication and serves as a critical target for antiviral drug development.

methodsA fluorescence resonance energy transfer (FRET)-based high-throughput screening (HTS) platform was developed to identify 2C helicase inhibitors. Primary screening evaluated 4424 compounds for helicase inhibition. Molecular docking analyzed inhibitor interactions with the N207 residue within the catalytic core and helicase inhibition assays classified the inhibitor type (mixed, competitive, noncompetitive). Differential scanning fluorimetry (nanoDSF) quantified 2C thermal destabilization. Antiviral activity was assessed via indirect immunofluorescence, RT-qPCR, and plaque reduction assays.

resultsSix compounds inhibited 2C helicase activity at >620 μM. Molecular docking revealed hydrogen bonding, hydrophobic interactions, and π-cation stabilization at the catalytic core. 2-MPO and MPPI were classified as mixed-type inhibitors, 5-TzS

conclusionsThe established FRET-based HTS platform targeting 2C helicase facilitates anti-FMDV lead discovery, while 2C inhibitors may serve as an effective therapeutic strategy against other picornaviruses.

Indexed as

Antiviral AgentsEnzyme InhibitorsFoot-and-Mouth Disease VirusRNA HelicasesSmall Molecule LibrariesViral Nonstructural ProteinsVirus ReplicationAnimalsCarrier ProteinsDrug DiscoveryFluorescence Resonance Energy TransferHigh-Throughput Screening AssaysMolecular Docking Simulation2C protein, viralAntiviral AgentsCarrier ProteinsEnzyme InhibitorsRNA HelicasesSmall Molecule LibrariesViral Nonstructural Proteins2C proteinantiviral inhibitorFMDVhelicase

Identifiers

PMID40573376
PMCPMC12197642

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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.