Evidence map›Paper›PMID 30212572›Full record

ArticlePLoS pathogens2018

Plant A20/AN1 protein serves as the important hub to mediate antiviral immunity.

Li Chang, Ho-Hsiung Chang, Jui-Che Chang, Hsiang-Chia Lu, Tan-Tung Wang, Duen-Wei Hsu, Yuh Tzean, An-Po Cheng, Yi-Shu Chiu, Hsin-Hung Yeh

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.7field-weighted citation impact, top 6% 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. TheLife (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Li ChangAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Ho-Hsiung ChangAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Jui-Che ChangAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Hsiang-Chia LuDepartment of Plant Pathology and Microbiology, National Taiwan University, Taipei, Taiwan.
Tan-Tung WangDepartment of Plant Pathology and Microbiology, National Taiwan University, Taipei, Taiwan.
Duen-Wei HsuDepartment of Biotechnology, National Kaohsiung Normal University, Kaohsiung, Taiwan.ORCID 0000-0001-5762-7806
Yuh TzeanAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
An-Po ChengAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Yi-Shu ChiuAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.
Hsin-Hung YehAgricultural Biotechnology Research Center, Academia Sinica, Taipei, Taiwan.ORCID 0000-0001-6765-2853
Agricultural Biotechnology Research Center, Academia Sinica · TWNational Taiwan University · TWNational Kaohsiung Normal University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Salicylic acid (SA) is a key phytohormone that mediates a broad spectrum of resistance against a diverse range of viruses; however, the downstream pathway of SA governed antiviral immune response remains largely to be explored. Here, we identified an orchid protein containing A20 and AN1 zinc finger domains, designated Pha13. Pha13 is up-regulated upon virus infection, and the transgenic monocot orchid and dicot Arabidopsis overexpressing orchid Pha13 conferred greater resistance to different viruses. In addition, our data showed that Arabidopsis homolog of Pha13, AtSAP5, is also involved in virus resistance. Pha13 and AtSAP5 are early induced by exogenous SA treatment, and participate in the expression of SA-mediated immune responsive genes, including the master regulator gene of plant immunity, NPR1, as well as NPR1-independent virus defense genes. SA also induced the proteasome degradation of Pha13. Functional domain analysis revealed that AN1 domain of Pha13 is involved in expression of orchid NPR1 through its AN1 domain, whereas dual A20/AN1 domains orchestrated the overall virus resistance. Subcellular localization analysis suggested that Pha13 can be found localized in the nucleus. Self-ubiquitination assay revealed that Pha13 confer E3 ligase activity, and the main E3 ligase activity was mapped to the A20 domain. Identification of Pha13 interacting proteins and substrate by yeast two-hybrid screening revealed mainly ubiquitin proteins. Further detailed biochemical analysis revealed that A20 domain of Pha13 binds to various polyubiquitin chains, suggesting that Pha13 may interact with multiple ubiquitinated proteins. Our findings revealed that Pha13 serves as an important regulatory hub in plant antiviral immunity, and uncover a delicate mode of immune regulation through the coordination of A20 and/or AN1 domains, as well as through the modulation of E3 ligase and ubiquitin chain binding activity of Pha13.

Indexed as

Plant ImmunityAmino Acid SequenceArabidopsisArabidopsis ProteinsGenes, PlantHost-Pathogen InteractionsModels, BiologicalOrchidaceaePlant ProteinsPlants, Genetically ModifiedPlant VirusesProtein BindingProtein DomainsSalicylic AcidSequence Homology, Amino AcidUbiquitinArabidopsis ProteinsPlant ProteinsSalicylic AcidUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID30212572
PMCPMC6155556
OpenAlexW2891202462

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.