Evidence map›Paper›PMID 32710986›Full record

ArticleJournal of molecular biology2020

Mutations Strengthened SARS-CoV-2 Infectivity.

Jiahui Chen, Rui Wang, Menglun Wang, Guo-Wei Wei

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 318 papers.

0numbers the graph read from it
0cells of the map it votes in
318citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

318 citing papers in PubMed, 510 citations in OpenAlex.

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  2. Persistent Stanley-Reisner Theory.Foundations of data science (Springfield, Mo.) · 2026
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  13. PERSISTENT DIRECTED FLAG LAPLACIAN.Foundations of data science (Springfield, Mo.) · 2025
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  15. Validation of a Traditional Medicine,Pharmaceuticals (Basel, Switzerland) · 2025
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  16. Article
  17. Review
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  19. Article
  20. Mayer-Homology Learning Prediction of Protein-Ligand Binding Affinities.Journal of computational biophysics and chemistry · 2025
    Article

258 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

4 authors at 1 institution in 1 country.

Jiahui ChenDepartment of Mathematics, Michigan State University, MI 48824, USA.
Rui WangDepartment of Mathematics, Michigan State University, MI 48824, USA.
Menglun WangDepartment of Mathematics, Michigan State University, MI 48824, USA.
Guo-Wei WeiDepartment of Mathematics, Michigan State University, MI 48824, USA; Department of Electrical and Computer Engineering, Michigan State University, MI 48824, USA; Department of Biochemistry and Molecular Biology, Michigan State University, MI 48824, USA. Electronic address: wei@math.msu.edu.
Michigan State University · US

Funding

Synergistic integration of topology and machine learning for the predictions of protein-ligand binding affinities and mutation impactsR01GM126189 · NIGMS · MICHIGAN STATE UNIVERSITY · PI WEI, GUOWEI · 2018 to 2021
$1.4M
NIGMS NIH HHS R01 GM126189
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectivity is a major concern in coronavirus disease 2019 (COVID-19) prevention and economic reopening. However, rigorous determination of SARS-CoV-2 infectivity is very difficult owing to its continuous evolution with over 10,000 single nucleotide polymorphisms (SNP) variants in many subtypes. We employ an algebraic topology-based machine learning model to quantitatively evaluate the binding free energy changes of SARS-CoV-2 spike glycoprotein (S protein) and host angiotensin-converting enzyme 2 receptor following mutations. We reveal that the SARS-CoV-2 virus becomes more infectious. Three out of six SARS-CoV-2 subtypes have become slightly more infectious, while the other three subtypes have significantly strengthened their infectivity. We also find that SARS-CoV-2 is slightly more infectious than SARS-CoV according to computed S protein-angiotensin-converting enzyme 2 binding free energy changes. Based on a systematic evaluation of all possible 3686 future mutations on the S protein receptor-binding domain, we show that most likely future mutations will make SARS-CoV-2 more infectious. Combining sequence alignment, probability analysis, and binding free energy calculation, we predict that a few residues on the receptor-binding motif, i.e., 452, 489, 500, 501, and 505, have high chances to mutate into significantly more infectious COVID-19 strains.

Indexed as

Evolution, MolecularMutationAmino Acid SequenceAngiotensin-Converting Enzyme 2BetacoronavirusCluster AnalysisCoronavirus InfectionsCOVID-19DNA Mutational AnalysisGenotypeGeographic MappingHumansMachine LearningModels, MolecularPandemicsPeptidyl-Dipeptidase AACE2 protein, humanAngiotensin-Converting Enzyme 2Peptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19mutationprotein-protein interactionspike proteinviral infectivity

Identifiers

PMID32710986
PMCPMC7375973
OpenAlexW3044722686

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.