Evidence map›Paper›PMID 34764391›Full record

ArticleScientific reports2021

Exposing structural variations in SARS-CoV-2 evolution.

Jiaan Yang, Peng Zhang, Wen Xiang Cheng, Youyong Lu, Wu Gang, Gang Ren

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 5 institutions in 2 countries.

Jiaan YangShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, Guangdong, China. jyang@micropht.com.
Peng ZhangShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, Guangdong, China.
Wen Xiang ChengShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, Guangdong, China.
Youyong LuLaboratory of Molecular Oncology, Peking University Cancer Hospital and Institute, Beijing, 100142, China.
Wu GangSchool of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, China.
Gang RenThe Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Shenzhen Institutes of Advanced Technology · CNChinese Academy of Sciences · CNHuazhong University of Science and Technology · CNLawrence Berkeley National Laboratory · USPeking University Cancer Hospital · CN

Funding

STRUCTURAL ANALYSIS OF THE MANNOSE 6-PHOSPHATE RECEPTORSR01DK042667 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI DAHMS, NANCY M. · 1997 to 2023
$9.8M
Synaptic Organizers: Dynamic Regulation of Trans-synaptic BridgesR01MH077303 · NIMH · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Gabrielle Rudenko · 2006 to 2026
$8.2M
Structure-Function Relationship Studies of the Plasma Lipid Transfer Proteins CETP and PLTPR01HL115153 · NHLBI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2012 to 2021
$3.9M
Lipoprotein Structure and Function by Individual Particle Electron TomographyR01GM104427 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI REN, GANG · 2013 to 2016
$1.3M
NHLBI NIH HHS R01 HL115153NIDDK NIH HHS R01 DK042667NIGMS NIH HHS R01 GM104427NIH HHS R01HL115153NIMH NIH HHS R01 MH077303
6 · The paper itself

Abstract

The mutation of SARS-CoV-2 influences viral function as residue replacements affect both physiochemical properties and folding conformations. Although a large amount of data on SARS-CoV-2 is available, the investigation of how viral functions change in response to mutations is hampered by a lack of effective structural analysis. Here, we exploit the advances of protein structure fingerprint technology to study the folding conformational changes induced by mutations. With integration of both protein sequences and folding conformations, the structures are aligned for SARS-CoV to SARS-CoV-2, including Alpha variant (lineage B.1.1.7) and Delta variant (lineage B.1.617.2). The results showed that the virus evolution with change in mutational positions and physicochemical properties increased the affinity between spike protein and ACE2, which plays a critical role in coronavirus entry into human cells. Additionally, these structural variations impact vaccine effectiveness and drug function over the course of SARS-CoV-2 evolution. The analysis of structural variations revealed how the coronavirus has gradually evolved in both structure and function and how the SARS-CoV-2 variants have contributed to more severe acute disease worldwide.

Indexed as

Evolution, MolecularMutationAmino Acid SequenceAngiotensin-Converting Enzyme 2COVID-19HumansModels, MolecularProtein ConformationProtein FoldingProtein Interaction MapsProtein MultimerizationSARS-CoV-2Sequence AlignmentSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID34764391
PMCPMC8586246
OpenAlexW3200554417

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.