Evidence map›Paper›PMID 25609249›Full record

ArticleThe Journal of biological chemistry2015

Structural view and substrate specificity of papain-like protease from avian infectious bronchitis virus.

Lingying Kong, Neil Shaw, Lingming Yan, Zhiyong Lou, Zihe Rao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.9field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Inhibiting Infectious Bronchitis Virus PLpro Using Ubiquitin Variants.International journal of molecular sciences · 2025
    Article
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  3. Review
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  7. Research Advances on Swine Acute Diarrhea Syndrome Coronavirus.Animals : an open access journal from MDPI · 2024
    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

5 authors at 2 institutions in 1 country.

Lingying KongFrom the Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, China.
Neil ShawCollege of Life Sciences, Nankai University, Tianjin 300071, China, and National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Lingming YanFrom the Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, China.
Zhiyong LouFrom the Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, China.
Zihe RaoFrom the Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, China, College of Life Sciences, Nankai University, Tianjin 300071, China, and National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China raozh@xtal.tsinghua.edu.cn.
Tsinghua University · CNNankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Papain-like protease (PLpro) of coronaviruses (CoVs) carries out proteolytic maturation of non-structural proteins that play a role in replication of the virus and performs deubiquitination of host cell factors to scuttle antiviral responses. Avian infectious bronchitis virus (IBV), the causative agent of bronchitis in chicken that results in huge economic losses every year in the poultry industry globally, encodes a PLpro. The substrate specificities of this PLpro are not clearly understood. Here, we show that IBV PLpro can degrade Lys(48)- and Lys(63)-linked polyubiquitin chains to monoubiquitin but not linear polyubiquitin. To explain the substrate specificities, we have solved the crystal structure of PLpro from IBV at 2.15-Å resolution. The overall structure is reminiscent of the structure of severe acute respiratory syndrome CoV PLpro. However, unlike the severe acute respiratory syndrome CoV PLpro that lacks blocking loop (BL) 1 of deubiquitinating enzymes, the IBV PLpro has a short BL1-like loop. Access to a conserved catalytic triad consisting of Cys(101), His(264), and Asp(275) is regulated by the flexible BL2. A model of ubiquitin-bound IBV CoV PLpro brings out key differences in substrate binding sites of PLpros. In particular, P3 and P4 subsites as well as residues interacting with the β-barrel of ubiquitin are different, suggesting different catalytic efficiencies and substrate specificities. We show that IBV PLpro cleaves peptide substrates KKAG-7-amino-4-methylcoumarin and LRGG-7-amino-4-methylcoumarin with different catalytic efficiencies. These results demonstrate that substrate specificities of IBV PLpro are different from other PLpros and that IBV PLpro might target different ubiquitinated host factors to aid the propagation of the virus.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCoronavirus InfectionsCrystallography, X-RayInfectious bronchitis virusModels, MolecularMolecular Sequence DataPapainPolyubiquitinPoultryPoultry DiseasesProtein ConformationSequence AlignmentSubstrate SpecificityUbiquitinPapainPolyubiquitinUbiquitinCrystal StructureEnzyme MechanismInfectious DiseaseProteaseVirus

Identifiers

PMID25609249
PMCPMC4358136
OpenAlexW2050632465

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.