SrasV1, PubMed, Curation, bibRecord, 000158

Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2.

Identifieur interne : 000158 ( PubMed/Curation ); précédent : 000157; suivant : 000159

Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2.

Auteurs : Jiahua He [République populaire de Chine] ; Huanyu Tao [République populaire de Chine] ; Yumeng Yan [République populaire de Chine] ; Sheng-You Huang [République populaire de Chine] ; Yi Xiao [République populaire de Chine]

Source :

Viruses [ 1999-4915 ] ; 2020.

RBID : pubmed:32290077

Descripteurs français

English descriptors

KwdEn :
- Betacoronavirus (metabolism), Biological Evolution, Coronavirus Infections (metabolism), Coronavirus Infections (virology), Hot Temperature, Humans, Molecular Docking Simulation, Molecular Dynamics Simulation, Pandemics, Peptidyl-Dipeptidase A (metabolism), Pneumonia, Viral (metabolism), Pneumonia, Viral (virology), Protein Binding, Protein Stability, SARS Virus (metabolism), Spike Glycoprotein, Coronavirus (metabolism).
MESH :
- chemical , metabolism : Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus.
- metabolism : Betacoronavirus, Coronavirus Infections, Pneumonia, Viral, SARS Virus.
- virology : Coronavirus Infections, Pneumonia, Viral.
- Biological Evolution, Hot Temperature, Humans, Molecular Docking Simulation, Molecular Dynamics Simulation, Pandemics, Protein Binding, Protein Stability.

Abstract

The outbreak of a novel coronavirus, which was later formally named the severe acute respiratory coronavirus 2 (SARS-CoV-2), has caused a worldwide public health crisis. Previous studies showed that SARS-CoV-2 is highly homologous to SARS-CoV and infects humans through the binding of the spike protein to ACE2. Here, we have systematically studied the molecular mechanisms of human infection with SARS-CoV-2 and SARS-CoV by protein-protein docking and MD simulations. It was found that SARS-CoV-2 binds ACE2 with a higher affinity than SARS-CoV, which may partly explain that SARS-CoV-2 is much more infectious than SARS-CoV. In addition, the spike protein of SARS-CoV-2 has a significantly lower free energy than that of SARS-CoV, suggesting that SARS-CoV-2 is more stable and may survive a higher temperature than SARS-CoV. This provides insights into the evolution of SARS-CoV-2 because SARS-like coronaviruses have originated in bats. Our computation also suggested that the RBD-ACE2 binding for SARS-CoV-2 is much more temperature-sensitive than that for SARS-CoV. Thus, it is expected that SARS-CoV-2 would decrease its infection ability much faster than SARS-CoV when the temperature rises. These findings would be beneficial for the disease prevention and drug/vaccine development of SARS-CoV-2.

DOI: 10.3390/v12040428
PubMed: 32290077

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The outbreak of a novel coronavirus, which was later formally named the severe acute respiratory coronavirus 2 (SARS-CoV-2), has caused a worldwide public health crisis. Previous studies showed that SARS-CoV-2 is highly homologous to SARS-CoV and infects humans through the binding of the spike protein to ACE2. Here, we have systematically studied the molecular mechanisms of human infection with SARS-CoV-2 and SARS-CoV by protein-protein docking and MD simulations. It was found that SARS-CoV-2 binds ACE2 with a higher affinity than SARS-CoV, which may partly explain that SARS-CoV-2 is much more infectious than SARS-CoV. In addition, the spike protein of SARS-CoV-2 has a significantly lower free energy than that of SARS-CoV, suggesting that SARS-CoV-2 is more stable and may survive a higher temperature than SARS-CoV. This provides insights into the evolution of SARS-CoV-2 because SARS-like coronaviruses have originated in bats. Our computation also suggested that the RBD-ACE2 binding for SARS-CoV-2 is much more temperature-sensitive than that for SARS-CoV. Thus, it is expected that SARS-CoV-2 would decrease its infection ability much faster than SARS-CoV when the temperature rises. These findings would be beneficial for the disease prevention and drug/vaccine development of SARS-CoV-2.</div>
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Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2.

Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2.

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