Cargando…

Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective

BACKGROUND: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has caused millions of infections and deaths worldwide since its discovery in late 2019 in Wuhan, China. The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein binds to the human angiotensin-converting enzyme-2 (ACE2...

Descripción completa

Detalles Bibliográficos
Autores principales: Borkotoky, Subhomoi, Dey, Debajit, Hazarika, Zaved
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9786537/
https://www.ncbi.nlm.nih.gov/pubmed/36562937
http://dx.doi.org/10.1007/s11033-022-08193-4
_version_ 1784858309478580224
author Borkotoky, Subhomoi
Dey, Debajit
Hazarika, Zaved
author_facet Borkotoky, Subhomoi
Dey, Debajit
Hazarika, Zaved
author_sort Borkotoky, Subhomoi
collection PubMed
description BACKGROUND: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has caused millions of infections and deaths worldwide since its discovery in late 2019 in Wuhan, China. The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein binds to the human angiotensin-converting enzyme-2 (ACE2) receptor, a critical component of the renin-angiotensin system (RAS) that initiates the viral transmission. Most of the critical mutations found in SARS-CoV-2 are associated with the RBD of the spike protein. These mutations have the potential to reduce the efficacy of vaccines and neutralizing antibodies. METHODS: In this review, the structural details of ACE2, RBD and their interactions are discussed. In addition, some critical mutations of RBD and their impact on ACE2-RBD interactions are also discussed. CONCLUSION: Preventing the interaction between Spike RBD and ACE2 is considered a viable therapeutic strategy since ACE2 binding by RBD is the first step in virus infection. Because the interactions between the two entities are critical for both viral transmission and therapeutic development, it is essential to understand their interactions in detail.
format Online
Article
Text
id pubmed-9786537
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Springer Netherlands
record_format MEDLINE/PubMed
spelling pubmed-97865372022-12-27 Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective Borkotoky, Subhomoi Dey, Debajit Hazarika, Zaved Mol Biol Rep Review BACKGROUND: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has caused millions of infections and deaths worldwide since its discovery in late 2019 in Wuhan, China. The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein binds to the human angiotensin-converting enzyme-2 (ACE2) receptor, a critical component of the renin-angiotensin system (RAS) that initiates the viral transmission. Most of the critical mutations found in SARS-CoV-2 are associated with the RBD of the spike protein. These mutations have the potential to reduce the efficacy of vaccines and neutralizing antibodies. METHODS: In this review, the structural details of ACE2, RBD and their interactions are discussed. In addition, some critical mutations of RBD and their impact on ACE2-RBD interactions are also discussed. CONCLUSION: Preventing the interaction between Spike RBD and ACE2 is considered a viable therapeutic strategy since ACE2 binding by RBD is the first step in virus infection. Because the interactions between the two entities are critical for both viral transmission and therapeutic development, it is essential to understand their interactions in detail. Springer Netherlands 2022-12-23 2023 /pmc/articles/PMC9786537/ /pubmed/36562937 http://dx.doi.org/10.1007/s11033-022-08193-4 Text en © The Author(s), under exclusive licence to Springer Nature B.V. 2022, Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Review
Borkotoky, Subhomoi
Dey, Debajit
Hazarika, Zaved
Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title_full Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title_fullStr Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title_full_unstemmed Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title_short Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
title_sort interactions of angiotensin-converting enzyme-2 (ace2) and sars-cov-2 spike receptor-binding domain (rbd): a structural perspective
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9786537/
https://www.ncbi.nlm.nih.gov/pubmed/36562937
http://dx.doi.org/10.1007/s11033-022-08193-4
work_keys_str_mv AT borkotokysubhomoi interactionsofangiotensinconvertingenzyme2ace2andsarscov2spikereceptorbindingdomainrbdastructuralperspective
AT deydebajit interactionsofangiotensinconvertingenzyme2ace2andsarscov2spikereceptorbindingdomainrbdastructuralperspective
AT hazarikazaved interactionsofangiotensinconvertingenzyme2ace2andsarscov2spikereceptorbindingdomainrbdastructuralperspective