Evidence map›Paper›PMID 35039570›Full record

ArticleScientific reports2022

Binding behavior of spike protein and receptor binding domain of the SARS-CoV-2 virus at different environmental conditions.

Meiyi Zhang, Haoqi Wang, Emma R Foster, Zivko L Nikolov, Sandun D Fernando, Maria D King

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Meiyi ZhangDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA.
Haoqi WangDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA.
Emma R FosterDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA.
Zivko L NikolovDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA.
Sandun D FernandoDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA.
Maria D KingDepartment of Biological and Agricultural Engineering, Texas A&M University, 2117 TAMU, College Station, TX, 77843, USA. mdking@tamu.edu.
Texas A&M University · US

Funding

National Science Foundation NSF CBET 2034048
6 · The paper itself

Abstract

A novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified as the cause of the COVID-19 pandemic that originated in China in December 2019. Although extensive research has been performed on SARS-CoV-2, the binding behavior of spike (S) protein and receptor binding domain (RBD) of SARS-CoV-2 at different environmental conditions have yet to be studied. The objective of this study is to investigate the effect of temperature, fatty acids, ions, and protein concentration on the binding behavior and rates of association and dissociation between the S protein and RBD of SARS-CoV-2 and the hydrophobic aminopropylsilane (APS) biosensors using biolayer interferometry (BLI) validated with molecular dynamics simulation. Our results suggest three conditions-high ionic concentration, presence of hydrophobic fatty acids, and low temperature-favor the attachment of S protein and RBD to hydrophobic surfaces. Increasing the temperature within an hour from 0 to 25 °C results in S protein detachment, suggesting that freezing can cause structural changes in the S protein, affecting its binding kinetics at higher temperature. At all the conditions, RBD exhibits lower dissociation capabilities than the full-length S trimer protein, indicating that the separated RBD formed stronger attachment to hydrophobic surfaces compared to when it was included in the S protein.

Indexed as

Spike Glycoprotein, CoronavirusBinding SitesBiosensing TechniquesCOVID-19KineticsProtein BindingProtein DomainsSpike Glycoprotein, Coronavirus

Identifiers

PMID35039570
PMCPMC8763896
OpenAlexW4205496594

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.