Evidence map›Paper›PMID 36851554›Full record

ReviewViruses2023

Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.

Priscila Sutto-Ortiz, Jean-François Eléouët, François Ferron, Etienne Decroly

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2023. 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
8.2field-weighted citation impact, top 2% of its field
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, 38 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Priscila Sutto-OrtizAix Marseille Université, CNRS, AFMB, UMR, 7257 Marseille, France.ORCID 0000-0001-8672-690X
Jean-François EléouëtUnité de Virologie et Immunologie Moléculaires, INRAE, Université Paris Saclay, F78350 Jouy en Josas, France.
François FerronAix Marseille Université, CNRS, AFMB, UMR, 7257 Marseille, France.ORCID 0000-0002-8351-4992
Etienne DecrolyAix Marseille Université, CNRS, AFMB, UMR, 7257 Marseille, France.
Centre National de la Recherche Scientifique · FRUniversité Paris-Saclay · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human respiratory syncytial virus (RSV) is a negative-sense, single-stranded RNA virus. It is the major cause of severe acute lower respiratory tract infection in infants, the elderly population, and immunocompromised individuals. There is still no approved vaccine or antiviral treatment against RSV disease, but new monoclonal prophylactic antibodies are yet to be commercialized, and clinical trials are in progress. Hence, urgent efforts are needed to develop efficient therapeutic treatments. RSV RNA synthesis comprises viral transcription and replication that are catalyzed by the large protein (L) in coordination with the phosphoprotein polymerase cofactor (P), the nucleoprotein (N), and the M2-1 transcription factor. The replication/transcription is orchestrated by the L protein, which contains three conserved enzymatic domains: the RNA-dependent RNA polymerase (RdRp), the polyribonucleotidyl transferase (PRNTase or capping), and the methyltransferase (MTase) domain. These activities are essential for the RSV replicative cycle and are thus considered as attractive targets for the development of therapeutic agents. In this review, we summarize recent findings about RSV L domains structure that highlight how the enzymatic activities of RSV L domains are interconnected, discuss the most relevant and recent antivirals developments that target the replication/transcription complex, and conclude with a perspective on identified knowledge gaps that enable new research directions.

Indexed as

NucleoproteinsRespiratory Syncytial Virus, HumanAgedAntibodies, MonoclonalAntiviral AgentsDNA-Directed RNA PolymerasesHumansInfantRNA-Dependent RNA PolymeraseTranscription FactorsAntibodies, MonoclonalAntiviral AgentsDNA-Directed RNA PolymerasesNucleoproteinsRNA-Dependent RNA PolymeraseTranscription Factorsantiviralcappingdrug designhuman respiratory syncytial virusmethyltransferasepolymerasepolyribonucleotidyl transferase

Identifiers

PMID36851554
PMCPMC9960070
OpenAlexW4318055118

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.