Evidence map›Paper›PMID 39837328›Full record

ArticleCell2025

Structural and functional analysis of the Nipah virus polymerase complex.

Side Hu, Heesu Kim, Pan Yang, Zishuo Yu, Barbara Ludeke, Shawna Mobilia, Junhua Pan, Margaret Stratton, Yuemin Bian, Rachel Fearns and 1 more

Abstract read
In one paragraph

Article in Cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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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.

Side HuDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Heesu KimDepartment of Virology, Immunology & Microbiology, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Pan YangDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Zishuo YuDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Barbara LudekeDepartment of Virology, Immunology & Microbiology, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Shawna MobiliaDepartment of Virology, Immunology & Microbiology, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Junhua PanBiomedical Research Institute and School of Life and Health Sciences, Hubei University of Technology, Wuhan, China.
Margaret StrattonDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
Yuemin BianSchool of Medicine, Shanghai University, Shanghai, China.
Rachel FearnsDepartment of Virology, Immunology & Microbiology, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA. Electronic address: rfearns@bu.edu.
Jonathan AbrahamDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA; Department of Medicine, Division of Infectious Diseases, Brigham & Women's Hospital, Boston, MA, USA; Center for Integrated Solutions in Infectious Diseases, Broad Institute of Harvard and MIT, Cambridge, MA, USA; Howard Hughes Medical Institute, Boston, MA, USA. Electronic address: jonathan_abraham@hms.harvard.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nipah virus (NiV) is a bat-borne, zoonotic RNA virus that is highly pathogenic in humans. The NiV polymerase, which mediates viral genome replication and mRNA transcription, is a promising drug target. We determined the cryoelectron microscopy (cryo-EM) structure of the NiV polymerase complex, comprising the large protein (L) and phosphoprotein (P), and performed structural, biophysical, and in-depth functional analyses of the NiV polymerase. The L protein assembles with a long P tetrameric coiled-coil that is capped by a bundle of ⍺-helices that we show are likely dynamic in solution. Docking studies with a known L inhibitor clarify mechanisms of antiviral drug resistance. In addition, we identified L protein features that are required for both transcription and RNA replication and mutations that have a greater impact on RNA replication than on transcription. Our findings have the potential to aid in the rational development of drugs to combat NiV infection.

Indexed as

Nipah VirusViral ProteinsAnimalsAntiviral AgentsCryoelectron MicroscopyDNA-Directed RNA PolymerasesHumansModels, MolecularMolecular Docking SimulationPhosphoproteinsTranscription, GeneticVirus ReplicationAntiviral AgentsDNA-Directed RNA PolymerasesPhosphoproteinsViral Proteinsemerging virusesNipah viruspolymeraseRNA replicationRNA transcriptionRNA virus

Identifiers

PMID39837328
PMCPMC11813165

What OpenQuestion holds

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Registered trials

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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.