Evidence map›Paper›PMID 33864728›Full record

ArticleThe FEBS journal2021

Host PDZ-containing proteins targeted by SARS-CoV-2.

Célia Caillet-Saguy, Fabien Durbesson, Veronica V Rezelj, Gergö Gogl, Quang Dinh Tran, Jean-Claude Twizere, Marco Vignuzzi, Renaud Vincentelli, Nicolas Wolff

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed, 72 citations in OpenAlex.

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  5. 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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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

9 authors at 2 institutions in 2 countries.

Célia Caillet-SaguyInstitut Pasteur, Unité Récepteurs-Canaux, UMR CNRS 3571, Paris, France.ORCID 0000-0001-5066-0435
Fabien DurbessonAFMB, UMR CNRS 7257, Marseille, France.
Veronica V RezeljInstitut Pasteur, Unité Populations Virales et Pathogénèse, UMR CNRS 3569, Paris, France.
Gergö GoglIGBMC, INSERM U1258/UMR CNRS 7104, Illkirch, France.
Quang Dinh TranInstitut Pasteur, Unité Populations Virales et Pathogénèse, UMR CNRS 3569, Paris, France.ORCID 0000-0002-9263-0733
Jean-Claude TwizereGIGA Institute, Molecular Biology of Diseases, Viral Interactomes laboratory, University of Liege, Belgium.
Marco VignuzziInstitut Pasteur, Unité Populations Virales et Pathogénèse, UMR CNRS 3569, Paris, France.
Renaud VincentelliAFMB, UMR CNRS 7257, Marseille, France.
Nicolas WolffInstitut Pasteur, Unité Récepteurs-Canaux, UMR CNRS 3571, Paris, France.ORCID 0000-0002-4950-706X
Centre National de la Recherche Scientifique · FRUniversity of Liège · BE

Funding

ANR Recherche Action Covid19-FRM PDZCoV2Fondation ARC pour la Recherche sur le CancerFrench Infrastructure for Integrated Structural Biology ANR-10-INSB-05-01URGENCE COVID-19 fundraising campaign of Institut Pasteur
6 · The paper itself

Abstract

Small linear motifs targeting protein interacting domains called PSD-95/Dlg/ZO-1 (PDZ) have been identified at the C terminus of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) proteins E, 3a, and N. Using a high-throughput approach of affinity-profiling against the full human PDZome, we identified sixteen human PDZ binders of SARS-CoV-2 proteins E, 3A, and N showing significant interactions with dissociation constants values ranging from 3 to 82 μm. Six of them (TJP1, PTPN13, HTRA1, PARD3, MLLT4, LNX2) are also recognized by SARS-CoV while three (NHERF1, MAST2, RADIL) are specific to SARS-CoV-2 E protein. Most of these SARS-CoV-2 protein partners are involved in cellular junctions/polarity and could be also linked to evasion mechanisms of the immune responses during viral infection. Among the binders of the SARS-CoV-2 proteins E, 3a, or N, seven significantly affect viral replication under knock down gene expression in infected cells. This PDZ profiling identifying human proteins potentially targeted by SARS-CoV-2 can help to understand the multifactorial severity of COVID19 and to conceive effective anti-coronaviral agents for therapeutic purposes.

Indexed as

Carrier ProteinsCoronavirus Nucleocapsid ProteinsCOVID-19Host-Pathogen InteractionsHumansKinesinsMyosinsPDZ DomainsProtein BindingProtein Interaction Domains and MotifsProtein Tyrosine Phosphatase, Non-Receptor Type 13SARS-CoV-2Viral Envelope ProteinsViroporin ProteinsVirus InternalizationVirus Replication3a protein, SARS-CoVAFDN protein, humanCarrier ProteinsCoronavirus Nucleocapsid ProteinsE protein, SARS coronavirusKinesinsLNX2 protein, humanMyosinsProtein Tyrosine Phosphatase, Non-Receptor Type 13PTPN13 protein, humanTJP1 protein, humanViral Envelope ProteinsViroporin ProteinsZonula Occludens-1 Protein3A and Nhuman PDZ libraryPDZ-binding motifPDZ-containing proteinSARS-CoV-2viral proteins Eviral replication

Identifiers

PMID33864728
PMCPMC8250131
OpenAlexW3156430862

What Socratic holds

Textmetadata
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 Socratic graph.