Evidence map›Paper›PMID 39125601›Full record

ArticleInternational journal of molecular sciences2024

A Comparative Analysis of SARS-CoV-2 Variants of Concern (VOC) Spike Proteins Interacting with hACE2 Enzyme.

Jiawei Chen, Lingtao Chen, Heng Quan, Soon Goo Lee, Kaniz Fatama Khan, Ying Xie, Qiaomu Li, Maria Valero, Zhiyu Dai, Yixin Xie

Abstract readComparative Study
In one paragraph

Article in International journal of molecular sciences, 2024. 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
–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

3 citing papers in PubMed.

  1. AI-Guided Binding Mechanisms and Molecular Dynamics for MERS-CoV.International journal of molecular sciences · 2026
    Article
  2. Article
  3. 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

10 authors.

Jiawei ChenCollege of Computing, Data Science and Society, University of California, Berkeley, CA 94720, USA.ORCID 0009-0005-3862-282X
Lingtao ChenCollege of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.
Heng QuanDepartment of Civil and Urban Engineering, New York University, Brooklyn, NY 10012, USA.
Soon Goo LeeDepartment of Molecular and Cellular Biology, Kennesaw State University, Kennesaw, GA 30144, USA.
Kaniz Fatama KhanDepartment of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA 30144, USA.
Ying XieCollege of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.
Qiaomu LiCollege of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.
Maria ValeroCollege of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.
Zhiyu DaiDivision of Pulmonary and Critical Care Medicine, John T. Milliken Department of Medicine, Washington University School of Medicine in St. Louis, St. Louis, MO 63110, USA.ORCID 0000-0002-2945-7923
Yixin XieCollege of Computing and Software Engineering, Kennesaw State University, Marietta, GA 30060, USA.ORCID 0000-0002-4436-3474

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In late 2019, the emergence of a novel coronavirus led to its identification as SARS-CoV-2, precipitating the onset of the COVID-19 pandemic. Many experimental and computational studies were performed on SARS-CoV-2 to understand its behavior and patterns. In this research, Molecular Dynamic (MD) simulation is utilized to compare the behaviors of SARS-CoV-2 and its Variants of Concern (VOC)-Alpha, Beta, Gamma, Delta, and Omicron-with the hACE2 protein. Protein structures from the Protein Data Bank (PDB) were aligned and trimmed for consistency using Chimera, focusing on the receptor-binding domain (RBD) responsible for ACE2 interaction. MD simulations were performed using Visual Molecular Dynamics (VMD) and Nanoscale Molecular Dynamics (NAMD2), and salt bridges and hydrogen bond data were extracted from the results of these simulations. The data extracted from the last 5 ns of the 10 ns simulations were visualized, providing insights into the comparative stability of each variant's interaction with ACE2. Moreover, electrostatics and hydrophobic protein surfaces were calculated, visualized, and analyzed. Our comprehensive computational results are helpful for drug discovery and future vaccine designs as they provide information regarding the vital amino acids in protein-protein interactions (PPIs). Our analysis reveals that the Original and Omicron variants are the two most structurally similar proteins. The Gamma variant forms the strongest interaction with hACE2 through hydrogen bonds, while Alpha and Delta form the most stable salt bridges; the Omicron is dominated by positive potential in the binding site, which makes it easy to attract the hACE2 receptor; meanwhile, the Original, Beta, Delta, and Omicron variants show varying levels of interaction stability through both hydrogen bonds and salt bridges, indicating that targeted therapeutic agents can disrupt these critical interactions to prevent SARS-CoV-2 infection.

Indexed as

Angiotensin-Converting Enzyme 2COVID-19Molecular Dynamics SimulationProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusBinding SitesHumansHydrogen BondingACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2angiotensin-converting enzyme 2binding affinitycoronavirusCOVID-19hACE2hydrogen bondsmolecular dynamicsprotein–protein interactionssalt bridgespike protein

Identifiers

PMID39125601
PMCPMC11311974

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.