Evidence map›Paper›PMID 33210300›Full record

ArticleProteins2021

Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and NL63 mild?

Puneet Rawat, Sherlyn Jemimah, P K Ponnuswamy, M Michael Gromiha

Abstract read
In one paragraph

Article in Proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

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  16. Host variations in SARS-CoV-2 infection.Turkish journal of biology = Turk biyoloji dergisi · 2021
    Review
  17. 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

4 authors.

Puneet RawatDepartment of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.
Sherlyn JemimahDepartment of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.
P K PonnuswamyDepartment of Physics, Bharathidasan University, Tiruchirapalli, India.
M Michael GromihaDepartment of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.ORCID https://orcid.org/0000-0002-1776-4096

Funding

Department of Science and Technology, Government of India MSC/2020/000319
6 · The paper itself

Abstract

Coronaviruses are responsible for several epidemics, including the 2002 SARS, 2012 MERS, and COVID-19. The emergence of recent COVID-19 pandemic due to SARS-CoV-2 virus in December 2019 has resulted in considerable research efforts to design antiviral drugs and other therapeutics against coronaviruses. In this context, it is crucial to understand the biophysical and structural features of the major proteins that are involved in virus-host interactions. In the current study, we have compared spike proteins from three strains of coronaviruses NL63, SARS-CoV, and SARS-CoV, known to bind human angiotensin-converting enzyme 2 (ACE2), in terms of sequence/structure conservation, hydrophobic cluster formation and importance of binding site residues. The study reveals that the severity of coronavirus strains correlates positively with the interaction area, surrounding hydrophobicity and interaction energy and inversely correlate with the flexibility of the binding interface. Also, we identify the conserved residues in the binding interface of spike proteins in all three strains. The systematic point mutations show that these conserved residues in the respective strains are evolutionarily favored at their respective positions. The similarities and differences in the spike proteins of the three viruses indicated in this study may help researchers to deeply understand the structural behavior, binding site properties and etiology of ACE2 binding, accelerating the screening of potential lead molecules and the development/repurposing of therapeutic drugs.

Indexed as

Coronavirus NL63, HumanSARS-CoV-2Severe acute respiratory syndrome-related coronavirusAngiotensin-Converting Enzyme 2Antiviral AgentsCoronavirus InfectionsCOVID-19DNA Mutational AnalysisHumansHydrophobic and Hydrophilic InteractionsLigandsModels, StatisticalMutationProtein BindingProtein ConformationSpecies SpecificityACE2 protein, humanAngiotensin-Converting Enzyme 2Antiviral AgentsLigandsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2 bindingcoronavirus spike proteinCOVID-19mutational analysisNL63SARSsurrounding hydrophobicity

Identifiers

PMID33210300
PMCPMC7753379

What OpenQuestion holds

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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.