Evidence map›Paper›PMID 34117354›Full record

ArticleCommunications biology2021

Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain.

Airah Javorsky, Patrick O Humbert, Marc Kvansakul

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  3. Evolutionarily divergent nidovirus with an exceptionally large genome identified in Pacific oysters undergoing mass mortality.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024
    Review
  13. Article
  14. Article
  15. SARS-CoV-2 E protein: Pathogenesis and potential therapeutic development.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023
    Review
  16. Viral subversion of the cell polarity regulator Scribble.Biochemical Society transactions · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Airah JavorskyDepartment of Biochemistry & Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Vic, Australia.
Patrick O HumbertDepartment of Biochemistry & Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Vic, Australia. p.humbert@latrobe.edu.au.ORCID 0000-0002-1366-6691
Marc KvansakulDepartment of Biochemistry & Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Vic, Australia. m.kvansakul@latrobe.edu.au.ORCID 0000-0003-2639-2498
La Trobe University · AUThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 infection leads to coronavirus disease 2019 (COVID-19), which is associated with severe and life-threatening pneumonia and respiratory failure. However, the molecular basis of these symptoms remains unclear. SARS-CoV-1 E protein interferes with control of cell polarity and cell-cell junction integrity in human epithelial cells by binding to the PALS1 PDZ domain, a key component of the Crumbs polarity complex. We show that C-terminal PDZ binding motifs of SARS-CoV-1 and SARS-CoV-2 E proteins bind the PALS1 PDZ domain with 29.6 and 22.8 μM affinity, whereas the related sequence from MERS-CoV did not bind. We then determined crystal structures of PALS1 PDZ domain bound to both SARS-CoV-1 and SARS-CoV-2 E protein PDZ binding motifs. Our findings establish the structural basis for SARS-CoV-1/2 mediated subversion of Crumbs polarity signalling and serve as a platform for the development of small molecule inhibitors to suppress SARS-CoV-1/2 mediated disruption of polarity signalling in epithelial cells.

Indexed as

PDZ DomainsAmino Acid SequenceCoronavirus Envelope ProteinsHumansMembrane ProteinsModels, MolecularNucleoside-Phosphate KinaseProtein BindingCoronavirus Envelope Proteinsenvelope protein, SARS-CoV-2Membrane ProteinsMPP5 protein, humanNucleoside-Phosphate Kinase

Identifiers

PMID34117354
PMCPMC8196010
OpenAlexW3172160435

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.