Evidence map›Paper›PMID 32891874›Full record

ArticleMicrobes and infection

Improved binding of SARS-CoV-2 Envelope protein to tight junction-associated PALS1 could play a key role in COVID-19 pathogenesis.

Flavio De Maio, Ettore Lo Cascio, Gabriele Babini, Michela Sali, Stefano Della Longa, Bruno Tilocca, Paola Roncada, Alessandro Arcovito, Maurizio Sanguinetti, Giovanni Scambia and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Microbes and infection. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 9% 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

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
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  3. Review
  4. SARS-CoV-2 Is an Electricity-Driven Virus.Reviews of physiology, biochemistry and pharmacology · 2025
    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

11 authors at 4 institutions in 1 country.

Flavio De MaioDipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy; Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Microbiologia, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Ettore Lo CascioDipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Gabriele BabiniDipartimento di Scienze della Salute della Donna, del Bambino e di Sanità Pubblica, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy. Electronic address: gabriele.babini@guest.policlinicogemelli.it.
Michela SaliDipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy; Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Microbiologia, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Stefano Della LongaDepartment of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, Italy.
Bruno TiloccaDepartment of Health Science, University "Magna Græcia" of Catanzaro, Viale Europa, 88100 Catanzaro, Italy.
Paola RoncadaDepartment of Health Science, University "Magna Græcia" of Catanzaro, Viale Europa, 88100 Catanzaro, Italy.
Alessandro ArcovitoDipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy; Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy.
Maurizio SanguinettiDipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy; Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Microbiologia, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Giovanni ScambiaDipartimento di Scienze della Salute della Donna, del Bambino e di Sanità Pubblica, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy; Dipartimento di Scienze della Vita e Sanità Pubblica - Sezione di Ginecologia ed Ostetricia, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Andrea UrbaniDipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario "A. Gemelli", IRCCS, Largo A. Gemelli 8, 00168 Roma, Italy; Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Largo Francesco Vito 1, 00168 Roma, Italy.
Università Cattolica del Sacro Cuore · ITMagna Graecia University · ITAgostino Gemelli University Polyclinic · ITUniversity of L'Aquila · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Envelope (E) protein of SARS-CoV-2 is the most enigmatic protein among the four structural ones. Most of its current knowledge is based on the direct comparison to the SARS E protein, initially mistakenly undervalued and subsequently proved to be a key factor in the ER-Golgi localization and in tight junction disruption. We compared the genomic sequences of E protein of SARS-CoV-2, SARS-CoV and the closely related genomes of bats and pangolins obtained from the GISAID and GenBank databases. When compared to the known SARS E protein, we observed a significant difference in amino acid sequence in the C-terminal end of SARS-CoV-2 E protein. Subsequently, in silico modelling analyses of E proteins conformation and docking provide evidences of a strengthened binding of SARS-CoV-2 E protein with the tight junction-associated PALS1 protein. Based on our computational evidences and on data related to SARS-CoV, we believe that SARS-CoV-2 E protein interferes more stably with PALS1 leading to an enhanced epithelial barrier disruption, amplifying the inflammatory processes, and promoting tissue remodelling. These findings raise a warning on the underestimated role of the E protein in the pathogenic mechanism and open the route to detailed experimental investigations.

Indexed as

Amino Acid SequenceAnimalsChiropteraCOVID-19Databases, GeneticHumansMembrane ProteinsMolecular Dynamics SimulationNucleoside-Phosphate KinasePangolinsSARS-CoV-2Severe acute respiratory syndrome-related coronavirusTight JunctionsViral Envelope ProteinsMembrane ProteinsMPP5 protein, humanNucleoside-Phosphate KinaseViral Envelope ProteinsCOVID-19Envelope proteinPALS1SARS-CoV-2Tight junctions

Identifiers

PMID32891874
PMCPMC7473260
OpenAlexW3082060340

What OpenQuestion 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 OpenQuestion graph.