Evidence map›Paper›PMID 26485389›Full record

SynthesisPLoS pathogens2015

Structure Elucidation of Coxsackievirus A16 in Complex with GPP3 Informs a Systematic Review of Highly Potent Capsid Binders to Enteroviruses.

Luigi De Colibus, Xiangxi Wang, Aloys Tijsma, Johan Neyts, John A B Spyrou, Jingshan Ren, Jonathan M Grimes, Gerhard Puerstinger, Pieter Leyssen, Elizabeth E Fry and 2 more

Abstract readSystematic Review
In one paragraph

Synthesis in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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  9. Review
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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

12 authors.

Luigi De ColibusDivision of Structural Biology, University of Oxford, Oxford, United Kingdom.
Xiangxi WangNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, China.
Aloys TijsmaLaboratory of Virology and Chemotherapy, Rega Institute for Medical Research, Leuven, Belgium.
Johan NeytsLaboratory of Virology and Chemotherapy, Rega Institute for Medical Research, Leuven, Belgium.
John A B SpyrouDivision of Structural Biology, University of Oxford, Oxford, United Kingdom.
Jingshan RenDivision of Structural Biology, University of Oxford, Oxford, United Kingdom.
Jonathan M GrimesDivision of Structural Biology, University of Oxford, Oxford, United Kingdom; Diamond Light Source, Didcot, United Kingdom.
Gerhard PuerstingerDepartment of Pharmaceutical Chemistry, University of Innsbruck, Innsbruck, Austria.
Pieter LeyssenLaboratory of Virology and Chemotherapy, Rega Institute for Medical Research, Leuven, Belgium.
Elizabeth E FryDivision of Structural Biology, University of Oxford, Oxford, United Kingdom.
Zihe RaoNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, China; Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, China.
David I StuartDivision of Structural Biology, University of Oxford, Oxford, United Kingdom; Diamond Light Source, Didcot, United Kingdom.

Funding

Medical Research Council G1000099Medical Research Council G1100525Medical Research Council MR/N00065X/1Wellcome TrustWellcome Trust 075491/Z/04
6 · The paper itself

Abstract

The replication of enterovirus 71 (EV71) and coxsackievirus A16 (CVA16), which are the major cause of hand, foot and mouth disease (HFMD) in children, can be inhibited by the capsid binder GPP3. Here, we present the crystal structure of CVA16 in complex with GPP3, which clarifies the role of the key residues involved in interactions with the inhibitor. Based on this model, in silico docking was performed to investigate the interactions with the two next-generation capsid binders NLD and ALD, which we show to be potent inhibitors of a panel of enteroviruses with potentially interesting pharmacological properties. A meta-analysis was performed using the available structural information to obtain a deeper insight into those structural features required for capsid binders to interact effectively and also those that confer broad-spectrum anti-enterovirus activity.

Indexed as

Models, MolecularAnimalsAntiviral AgentsCapsidCapsid ProteinsCell LineCoxsackievirus InfectionsCrystallography, X-RayEnterovirus A, HumanHumansAntiviral AgentsCapsid Proteins

Identifiers

PMID26485389
PMCPMC4613828

What OpenQuestion holds

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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.