Evidence map›Paper›PMID 32825063›Full record

ArticleViruses2020

The Sialoside-Binding Pocket of SARS-CoV-2 Spike Glycoprotein Structurally Resembles MERS-CoV.

Mayanka Awasthi, Sahil Gulati, Debi P Sarkar, Swasti Tiwari, Suneel Kateriya, Peeyush Ranjan, Santosh Kumar Verma

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.7field-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

40 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  3. Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026
    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

7 authors at 4 institutions in 2 countries.

Mayanka AwasthiDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.ORCID 0000-0002-4395-0589
Sahil GulatiGatan Inc., Pleasanton, CA 94588, USA.ORCID 0000-0002-8255-479X
Debi P SarkarDepartment of Biochemistry, University of Delhi South Campus, New Delhi 110021, India.ORCID 0000-0002-8886-8415
Swasti TiwariDepartment of Molecular Medicine & Biotechnology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow 226014, India.ORCID 0000-0002-1701-2636
Suneel KateriyaSchool of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India.ORCID 0000-0001-5428-4297
Peeyush RanjanDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.
Santosh Kumar VermaDepartment of Molecular Medicine & Biotechnology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, Lucknow 226014, India.ORCID 0000-0001-6058-6494
Sanjay Gandhi Post Graduate Institute of Medical Sciences · INUniversity of Maryland, College Park · USJawaharlal Nehru University · INUniversity of Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

COVID-19 novel coronavirus (CoV) disease caused by severe acquired respiratory syndrome (SARS)-CoV-2 manifests severe lethal respiratory illness in humans and has recently developed into a worldwide pandemic. The lack of effective treatment strategy and vaccines against the SARS-CoV-2 poses a threat to human health. An extremely high infection rate and multi-organ secondary infection within a short period of time makes this virus more deadly and challenging for therapeutic interventions. Despite high sequence similarity and utilization of common host-cell receptor, human angiotensin-converting enzyme-2 (ACE2) for virus entry, SARS-CoV-2 is much more infectious than SARS-CoV. Structure-based sequence comparison of the N-terminal domain (NTD) of the spike protein of Middle East respiratory syndrome (MERS)-CoV, SARS-CoV, and SARS-CoV-2 illustrate three divergent loop regions in SARS-CoV-2, which is reminiscent of MERS-CoV sialoside binding pockets. Comparative binding analysis with host sialosides revealed conformational flexibility of SARS-CoV-2 divergent loop regions to accommodate diverse glycan-rich sialosides. These key differences with SARS-CoV and similarity with MERS-CoV suggest an evolutionary adaptation of SARS-CoV-2 spike glycoprotein reciprocal interaction with host surface sialosides to infect host cells with wide tissue tropism.

Indexed as

Amino SugarsBetacoronavirusBinding SitesMiddle East Respiratory Syndrome CoronavirusModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationN-Acetylneuraminic AcidProtein BindingProtein DomainsReceptors, CoronavirusReceptors, VirusSARS-CoV-2Severe acute respiratory syndrome-related coronavirusSialic AcidsSialyl Lewis X AntigenAmino SugarsN-Acetylneuraminic AcidReceptors, CoronavirusReceptors, VirusSialic AcidsSialyl Lewis X Antigensialyl-N-acetyllactosamineSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, SARS-CoV-2MERS-CoVN-terminal domainSARS-CoV-2spike glycoprotein

Identifiers

PMID32825063
PMCPMC7551769
OpenAlexW3049098896

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.