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SARS-CoV-2 virus-host interaction: currently available structures and implications of variant emergence on infectivity and immune response

Queirós-Reis, Luís, Gomes da Silva, Priscilla, Gonçalves, José, Brancale, Andrea, Bassetto, Marcella and Mesquita, João R. 2021. SARS-CoV-2 virus-host interaction: currently available structures and implications of variant emergence on infectivity and immune response. International Journal of Molecular Sciences 22 (19) , 10836. 10.3390/ijms221910836

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Abstract

Coronavirus disease 19, or COVID-19, is an infection associated with an unprecedented worldwide pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), which has led to more than 215 million infected people and more than 4.5 million deaths worldwide. SARS-CoV-2 cell infection is initiated by a densely glycosylated spike (S) protein, a fusion protein, binding human angiotensin converting enzyme 2 (hACE2), that acts as the functional receptor through the receptor binding domain (RBD). In this article, the interaction of hACE2 with the RBD and how fusion is initiated after recognition are explored, as well as how mutations influence infectivity and immune response. Thus, we focused on all structures available in the Protein Data Bank for the interaction between SARS-CoV-2 S protein and hACE2. Specifically, the Delta variant carries particular mutations associated with increased viral fitness through decreased antibody binding, increased RBD affinity and altered protein dynamics. Combining both existing mutations and mutagenesis studies, new potential SARS-CoV-2 variants, harboring advantageous S protein mutations, may be predicted. These include mutations S13I and W152C, decreasing antibody binding, N460K, increasing RDB affinity, or Q498R, positively affecting both properties.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Pharmacy
Additional Information: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/
Publisher: MDPI
ISSN: 1422-0067
Date of First Compliant Deposit: 20 October 2021
Date of Acceptance: 1 October 2021
Last Modified: 25 Oct 2021 11:00
URI: https://orca.cardiff.ac.uk/id/eprint/144960

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Cited 3 times in Scopus. View in Scopus. Powered By Scopus® Data

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