Evidence map›Paper›PMID 32005959›Full record

ArticleScientific reports2020

Structural basis for Glycan-receptor binding by mumps virus hemagglutinin-neuraminidase.

Rosa Ester Forgione, Cristina Di Carluccio, Marie Kubota, Yoshiyuki Manabe, Koichi Fukase, Antonio Molinaro, Takao Hashiguchi, Roberta Marchetti, Alba Silipo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

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  14. Antiviral Activity of CD437 Against Mumps Virus.Frontiers in microbiology · 2021
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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

9 authors at 3 institutions in 2 countries.

Rosa Ester Forgione *Department of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy.
Cristina Di Carluccio *Department of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy.
Marie KubotaDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka, 812-8582, Japan.
Yoshiyuki ManabeCore for Medicine and Science Collaborative Research and Education, Project Research Center for Fundamental Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka, 560-0043, Japan.
Koichi FukaseCore for Medicine and Science Collaborative Research and Education, Project Research Center for Fundamental Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka, 560-0043, Japan.
Antonio MolinaroDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy.
Takao HashiguchiDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka, 812-8582, Japan.
Roberta MarchettiDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy. roberta.marchetti@unina.it.
Alba SilipoDepartment of Chemical Sciences, Complesso Universitario Monte Sant'Angelo, University of Naples Federico II, Via Cintia 4, I-80126, Napoli, Italy. alba.silipo@unina.it.
University of Naples Federico II · ITOsaka University · JPKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mumps virus is one of the main cause of respiratory illnesses in humans, especially children. Among the viral surface glycoproteins, the hemagglutinin - neuraminidase, MuV-HN, plays key roles in virus entry into host cells and infectivity, thus representing an ideal target for the design of novel inhibitors. Here we report the detailed analysis of the molecular recognition of host cell surface sialylated glycans by the viral glycoprotein MuV-HN. By a combined use of NMR, docking, molecular modelling and CORCEMA-ST, the structural features of sialoglycans/MuV-HN complexes were revealed. Evidence for a different enzyme activity toward longer and complex substrates compared to unbranched ligands was also examined by an accurate NMR kinetic analysis. Our results provide the basis for the structure-based design of effective drugs against mumps-induced diseases.

Indexed as

Binding SitesHemagglutininsHumansKineticsMagnetic Resonance SpectroscopyMolecular Docking SimulationMumps virusNeuraminidasePolysaccharidesProtein ConformationViral Structural ProteinsHemagglutininsNeuraminidasePolysaccharidesViral Structural Proteins

Identifiers

PMID32005959
PMCPMC6994497
OpenAlexW3003205218

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.