Evidence map›Paper›PMID 33090512›Full record

ArticleJournal of medical virology2021

Effects of SARS-CoV-2 mutations on protein structures and intraviral protein-protein interactions.

Siqi Wu, Chang Tian, Panpan Liu, Dongjie Guo, Wei Zheng, Xiaoqiang Huang, Yang Zhang, Lijun Liu

Open access · bronzeAbstract read
In one paragraph

Article in Journal of medical virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
2.7field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Recent Progress of Protein Tertiary Structure Prediction.Molecules (Basel, Switzerland) · 2024
    Review
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7 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

8 authors at 2 institutions in 2 countries.

Siqi WuCollege of Life and Health Sciences, Northeastern University, Shenyang, Liaoning, China.
Chang TianCollege of Life and Health Sciences, Northeastern University, Shenyang, Liaoning, China.
Panpan LiuCollege of Life and Health Sciences, Northeastern University, Shenyang, Liaoning, China.
Dongjie GuoCollege of Life and Health Sciences, Northeastern University, Shenyang, Liaoning, China.
Wei ZhengDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.ORCID 0000-0002-2984-9003
Xiaoqiang HuangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.
Yang ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, USA.
Lijun LiuCollege of Life and Health Sciences, Northeastern University, Shenyang, Liaoning, China.ORCID 0000-0002-0027-4525
Northeastern University · CNUniversity of Michigan · US

Funding

Northeastern University N2020006Organization Department of Liaoning Province XLYC1907052
6 · The paper itself

Abstract

Since 2019, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causing coronavirus disease 2019 (COVID-19) has infected 10 millions of people across the globe, and massive mutations in virus genome have occurred during the rapid spread of this novel coronavirus. Variance in protein sequence might lead to a change in protein structure and interaction, then further affect the viral physiological characteristics, which could bring tremendous influence on the pandemic. In this study, we investigated 20 nonsynonymous mutations in the SARS-CoV-2 genome in which incidence rates were all ≥ 1% as of September 1st, 2020, and then modeled and analyzed the mutant protein structures. The results showed that four types of mutations caused dramatic changes in protein structures (RMSD ≥ 5.0 Å), which were Q57H and G251V in open-reading frames 3a (ORF3a), S194L, and R203K/G204R in nucleocapsid (N). Next, we found that these mutations also affected the binding affinity of intraviral protein interactions. In addition, the hot spots within these docking mutant complexes were altered, among which the mutation Q57H was involved in both Orf3a-S and Orf3a-Orf8 protein interactions. Besides, these mutations were widely distributed all over the world, and their occurrences fluctuated as time went on. Notably, the incidences of R203K/G204R in N and Q57H in Orf3a were both over 50% in some countries. Overall, our findings suggest that SARS-CoV-2 mutations could change viral protein structure, binding affinity, and hot spots of the interface, thereby might have impacts on SARS-CoV-2 transmission, diagnosis, and treatment of COVID-19.

Indexed as

Genome, ViralCOVID-19HumansMutationOpen Reading FramesProtein BindingProtein Structure, TertiarySARS-CoV-2Viral ProteinsViral Proteinsmutationprotein-protein interactionprotein structureSARS-CoV-2

Identifiers

PMID33090512
PMCPMC7675365
OpenAlexW3093085773

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.