Evidence map›Paper›PMID 33264497›Full record

ArticleThe FEBS journal2021

The structural basis of accelerated host cell entry by SARS-CoV-2†.

Murat Seyran, Kazuo Takayama, Vladimir N Uversky, Kenneth Lundstrom, Giorgio Palù, Samendra P Sherchan, Diksha Attrish, Nima Rezaei, Alaa A A Aljabali, Shinjini Ghosh and 14 more

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 109 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed, 2 pooled it
3.7field-weighted citation impact, top 4% 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

109 citing papers in PubMed, 2 syntheses or guidelines pooled it, 174 citations in OpenAlex.

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49 more citing papers are in PubMed but not listed here.

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

24 authors at 20 institutions in 14 countries.

Murat SeyranDoctoral Studies in Natural and Technical Sciences (SPL 44), University of Vienna, Austria.
Kazuo TakayamaCenter for iPS Cell Research and Application, Kyoto University, Japan.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Kenneth LundstromPanTherapeutics, Lutry, Switzerland.
Giorgio PalùDepartment of Molecular Medicine, University of Padova, Italy.
Samendra P SherchanDepartment of Environmental Health Sciences, Tulane University, New Orleans, LA, USA.
Diksha AttrishDr. B R Ambedkar Center for Biomedical Research (ACBR), University of Delhi (North Camps), Delhi, India.
Nima RezaeiResearch Center for Immunodeficiencies, Pediatrics Center of Excellence, Children's Medical Center, Tehran University of Medical Sciences, Iran.
Alaa A A AljabaliDepartment of Pharmaceutics and Pharmaceutical Technology, Faculty of Pharmacy, Yarmouk University, Irbid, Jordan.
Shinjini GhoshDepartment of Biophysics, Molecular Biology and Bioinformatics, University of Calcutta, Kolkata, India.
Damiano PizzolItalian Agency for Development Cooperation - Khartoum, Al Amarat, Sudan.
Gaurav ChauhanSchool of Engineering and Sciences, Tecnologico de Monterrey, Mexico.
Parise AdadiDepartment of Food Science, University of Otago, Dunedin, New Zealand.
Tarek Mohamed Abd El-AzizDepartment of Cellular and Integrative Physiology, University of Texas Health Science Center at San Antonio, TX, USA.ORCID 0000-0002-3441-9673
Antonio G SoaresZoology Department, Faculty of Science, Minia University, El-Minia, Egypt.
Ramesh KandimallaApplied Biology, CSIR-Indian Institute of Chemical Technology, Tarnaka, India.
Murtaza TambuwalaSchool of Pharmacy and Pharmaceutical Science, Ulster University, Coleraine, UK.
Sk Sarif HassanDepartment of Mathematics, Pingla Thana Mahavidyalaya, Paschim Medinipur, India.
Gajendra Kumar AzadDepartment of Zoology, Patna University, India.ORCID 0000-0001-5478-526X
Pabitra Pal ChoudhuryApplied Statistics Unit, Indian Statistical Institute, Kolkata, India.
Wagner Baetas-da-CruzTranslational Laboratory in Molecular Physiology, Centre for Experimental Surgery, College of Medicine, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Ángel Serrano-ArocaBiomaterials and Bioengineering Lab, Centro de Investigación Traslacional San Alberto Magno, Universidad Católica de Valencia San Vicente Mártir, Valencia, Spain.
Adam M BrufskyDepartment of Medicine, Division of Hematology/Oncology, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Bruce D UhalDepartment of Physiology, Michigan State University, East Lansing, MI, USA.ORCID 0000-0002-5201-432X
Education and Research Network · INIndian Statistical Institute · INKakatiya University · INKanya Maha Vidyalaya · INKyoto University · JPMichigan State University · USMinia University · EGNorwegian Agency for Development Cooperation · NOPatna University · INTecnológico de Monterrey · MXThe University of Texas Health Science Center at San Antonio · USTulane University · USUniversidade Federal do Rio de Janeiro · BRUniversity of Calcutta · INUniversity of Delhi · INUniversity of Otago · NZUniversity of Padua · ITUniversity of South Florida · USUniversity of Ulster · GBUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the pandemic coronavirus disease 2019 (COVID-19) that exhibits an overwhelming contagious capacity over other human coronaviruses (HCoVs). This structural snapshot describes the structural bases underlying the pandemic capacity of SARS-CoV-2 and explains its fast motion over respiratory epithelia that allow its rapid cellular entry. Based on notable viral spike (S) protein features, we propose that the flat sialic acid-binding domain at the N-terminal domain (NTD) of the S1 subunit leads to more effective first contact and interaction with the sialic acid layer over the epithelium, and this, in turn, allows faster viral 'surfing' of the epithelium and receptor scanning by SARS-CoV-2. Angiotensin-converting enzyme 2 (ACE-2) protein on the epithelial surface is the primary entry receptor for SARS-CoV-2, and protein-protein interaction assays demonstrate high-affinity binding of the spike protein (S protein) to ACE-2. To date, no high-frequency mutations were detected at the C-terminal domain of the S1 subunit in the S protein, where the receptor-binding domain (RBD) is located. Tight binding to ACE-2 by a conserved viral RBD suggests the ACE2-RBD interaction is likely optimal. Moreover, the viral S subunit contains a cleavage site for furin and other proteases, which accelerates cell entry by SARS-CoV-2. The model proposed here describes a structural basis for the accelerated host cell entry by SARS-CoV-2 relative to other HCoVs and also discusses emerging hypotheses that are likely to contribute to the development of antiviral strategies to combat the pandemic capacity of SARS-CoV-2.

Indexed as

Angiotensin-Converting Enzyme 2Antiviral AgentsBinding SitesCOVID-19Host-Pathogen InteractionsHumansPandemicsProtein BindingProtein DomainsReceptors, VirusRespiratory MucosaSARS-CoV-2Spike Glycoprotein, CoronavirusVirus AttachmentVirus InternalizationACE2 protein, humanAngiotensin-Converting Enzyme 2Antiviral AgentsReceptors, VirusSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVCOVID-19furin proteasereceptor-binding domainSARS-CoV-2sialic acid-binding domain

Identifiers

PMID33264497
PMCPMC7753708
OpenAlexW3107327505

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.