Evidence map›Paper›PMID 27089358›Full record

ArticleViruses2016

Purification and Biochemical Characterisation of Rabbit Calicivirus RNA-Dependent RNA Polymerases and Identification of Non-Nucleoside Inhibitors.

Nadya Urakova, Natalie Netzler, Andrew G Kelly, Michael Frese, Peter A White, Tanja Strive

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2016. 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
2.2field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 21 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

6 authors at 2 institutions in 1 country.

Nadya UrakovaCommonwealth Scinetific and Industrial Research Organisation, Health and Biosecurity, 2601 Canberra, ACT, Australia. nadezda.urakova@csiro.au.
Natalie NetzlerSchool of Biotechnology and Biomolecular Sciences, Faculty of Science, University of New South Wales, 2052 Sydney, NSW, Australia. n.netzler@unsw.edu.au.
Andrew G KellySchool of Biotechnology and Biomolecular Sciences, Faculty of Science, University of New South Wales, 2052 Sydney, NSW, Australia. agk22000@gmail.com.
Michael FreseCommonwealth Scinetific and Industrial Research Organisation, Health and Biosecurity, 2601 Canberra, ACT, Australia. michael.frese@canberra.edu.au.
Peter A WhiteSchool of Biotechnology and Biomolecular Sciences, Faculty of Science, University of New South Wales, 2052 Sydney, NSW, Australia. p.white@unsw.edu.au.
Tanja StriveCommonwealth Scinetific and Industrial Research Organisation, Health and Biosecurity, 2601 Canberra, ACT, Australia. tanja.strive@csiro.au.
University of Canberra · AUUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rabbit haemorrhagic disease virus (RHDV) is a calicivirus that causes acute infections in both domestic and wild European rabbits (Oryctolagus cuniculus). The virus causes significant economic losses in rabbit farming and reduces wild rabbit populations. The recent emergence of RHDV variants capable of overcoming immunity to other strains emphasises the need to develop universally effective antivirals to enable quick responses during outbreaks until new vaccines become available. The RNA-dependent RNA polymerase (RdRp) is a primary target for the development of such antiviral drugs. In this study, we used cell-free in vitro assays to examine the biochemical characteristics of two rabbit calicivirus RdRps and the effects of several antivirals that were previously identified as human norovirus RdRp inhibitors. The non-nucleoside inhibitor NIC02 was identified as a potential scaffold for further drug development against rabbit caliciviruses. Our experiments revealed an unusually high temperature optimum (between 40 and 45 °C) for RdRps derived from both a pathogenic and a non-pathogenic rabbit calicivirus, possibly demonstrating an adaptation to a host with a physiological body temperature of more than 38 °C. Interestingly, the in vitro polymerase activity of the non-pathogenic calicivirus RdRp was at least two times higher than that of the RdRp of the highly virulent RHDV.

Indexed as

Drug DiscoveryAmino Acid MotifsAmino Acid SequenceAnimalsAntiviral AgentsCaliciviridae InfectionsDose-Response Relationship, DrugEnzyme ActivationEvolution, MolecularGene ExpressionHemorrhagic Disease Virus, RabbitInhibitory Concentration 50KineticsRecombinant Fusion ProteinsRecombination, GeneticRNA-Dependent RNA PolymeraseAntiviral AgentsRecombinant Fusion ProteinsRNA-Dependent RNA Polymeraseantiviral agentsnon-nucleoside inhibitorspolymeraseRCV-A1RHDV

Identifiers

PMID27089358
PMCPMC4848594
OpenAlexW2338278816

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.