Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2.
During replication, some mutations occur in SARS-CoV-2, the causal agent of COVID-19, leading to the emergence of different variants of the virus. The mutations that accrue in different variants of the virus, influence the virus' ability to bind to human cell receptors and ability to evade the...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2023-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0291210&type=printable |
| _version_ | 1797682712200347648 |
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| author | Farzaneh Jafary Farzane Abasi Joozdani Kiana Shahzamani Sepideh Jafari Hossein Mirhendi Mohamad Reza Ganjalikhany |
| author_facet | Farzaneh Jafary Farzane Abasi Joozdani Kiana Shahzamani Sepideh Jafari Hossein Mirhendi Mohamad Reza Ganjalikhany |
| author_sort | Farzaneh Jafary |
| collection | DOAJ |
| description | During replication, some mutations occur in SARS-CoV-2, the causal agent of COVID-19, leading to the emergence of different variants of the virus. The mutations that accrue in different variants of the virus, influence the virus' ability to bind to human cell receptors and ability to evade the human immune system, the rate of viral transmission, and effectiveness of vaccines. Some of these mutations occur in the receptor binding domain (RBD) of the spike protein that may change the affinity of the virus for the ACE2 receptor. In this study, several in silico techniques, such as MD and SMD simulations, were used to perform comparative studies to deeply understand the effect of mutation on structural and functional details of the interaction of the spike glycoprotein of SARS-CoV-2, with the ACE2 receptor. According to our results, the mutation in the RBD associated with the Omicron variant increase binding affinity of the virus to ACE2 when compared to wild type and Delta variants. We also observed that the flexibility of the spike protein of the Omicron variant was lower than in comparison to other variants. In summary, different mutations in variants of the virus can have an effect on the binding mechanism of the receptor binding domain of the virus with ACE2. |
| first_indexed | 2024-03-12T00:03:49Z |
| format | Article |
| id | doaj.art-0e207fefc99e441fa5115c3bf2af42d1 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-03-12T00:03:49Z |
| publishDate | 2023-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-0e207fefc99e441fa5115c3bf2af42d12023-09-17T05:31:17ZengPublic Library of Science (PLoS)PLoS ONE1932-62032023-01-01189e029121010.1371/journal.pone.0291210Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2.Farzaneh JafaryFarzane Abasi JoozdaniKiana ShahzamaniSepideh JafariHossein MirhendiMohamad Reza GanjalikhanyDuring replication, some mutations occur in SARS-CoV-2, the causal agent of COVID-19, leading to the emergence of different variants of the virus. The mutations that accrue in different variants of the virus, influence the virus' ability to bind to human cell receptors and ability to evade the human immune system, the rate of viral transmission, and effectiveness of vaccines. Some of these mutations occur in the receptor binding domain (RBD) of the spike protein that may change the affinity of the virus for the ACE2 receptor. In this study, several in silico techniques, such as MD and SMD simulations, were used to perform comparative studies to deeply understand the effect of mutation on structural and functional details of the interaction of the spike glycoprotein of SARS-CoV-2, with the ACE2 receptor. According to our results, the mutation in the RBD associated with the Omicron variant increase binding affinity of the virus to ACE2 when compared to wild type and Delta variants. We also observed that the flexibility of the spike protein of the Omicron variant was lower than in comparison to other variants. In summary, different mutations in variants of the virus can have an effect on the binding mechanism of the receptor binding domain of the virus with ACE2.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0291210&type=printable |
| spellingShingle | Farzaneh Jafary Farzane Abasi Joozdani Kiana Shahzamani Sepideh Jafari Hossein Mirhendi Mohamad Reza Ganjalikhany Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. PLoS ONE |
| title | Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. |
| title_full | Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. |
| title_fullStr | Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. |
| title_full_unstemmed | Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. |
| title_short | Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2. |
| title_sort | different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of sars cov 2 spike protein in interaction with ace2 |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0291210&type=printable |
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