Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.

The SARS-CoV-2 pandemic highlights the need for a detailed molecular understanding of protective antibody responses. This is underscored by the emergence and spread of SARS-CoV-2 variants, including Alpha (B.1.1.7) and Delta (B.1.617.2), some of which appear to be less effectively targeted by curren...

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Autores principales:	Rui Yin, Johnathan D Guest, Ghazaleh Taherzadeh, Ragul Gowthaman, Ipsa Mittra, Jane Quackenbush, Brian G Pierce
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e124a4e516d34a9fbdf3e223838d242e
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spelling	oai:doaj.org-article:e124a4e516d34a9fbdf3e223838d242e2021-12-02T19:58:14ZStructural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.1553-734X1553-735810.1371/journal.pcbi.1009380https://doaj.org/article/e124a4e516d34a9fbdf3e223838d242e2021-09-01T00:00:00Zhttps://doi.org/10.1371/journal.pcbi.1009380https://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358The SARS-CoV-2 pandemic highlights the need for a detailed molecular understanding of protective antibody responses. This is underscored by the emergence and spread of SARS-CoV-2 variants, including Alpha (B.1.1.7) and Delta (B.1.617.2), some of which appear to be less effectively targeted by current monoclonal antibodies and vaccines. Here we report a high resolution and comprehensive map of antibody recognition of the SARS-CoV-2 spike receptor binding domain (RBD), which is the target of most neutralizing antibodies, using computational structural analysis. With a dataset of nonredundant experimentally determined antibody-RBD structures, we classified antibodies by RBD residue binding determinants using unsupervised clustering. We also identified the energetic and conservation features of epitope residues and assessed the capacity of viral variant mutations to disrupt antibody recognition, revealing sets of antibodies predicted to effectively target recently described viral variants. This detailed structure-based reference of antibody RBD recognition signatures can inform therapeutic and vaccine design strategies.Rui YinJohnathan D GuestGhazaleh TaherzadehRagul GowthamanIpsa MittraJane QuackenbushBrian G PiercePublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 17, Iss 9, p e1009380 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Rui Yin Johnathan D Guest Ghazaleh Taherzadeh Ragul Gowthaman Ipsa Mittra Jane Quackenbush Brian G Pierce Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
description	The SARS-CoV-2 pandemic highlights the need for a detailed molecular understanding of protective antibody responses. This is underscored by the emergence and spread of SARS-CoV-2 variants, including Alpha (B.1.1.7) and Delta (B.1.617.2), some of which appear to be less effectively targeted by current monoclonal antibodies and vaccines. Here we report a high resolution and comprehensive map of antibody recognition of the SARS-CoV-2 spike receptor binding domain (RBD), which is the target of most neutralizing antibodies, using computational structural analysis. With a dataset of nonredundant experimentally determined antibody-RBD structures, we classified antibodies by RBD residue binding determinants using unsupervised clustering. We also identified the energetic and conservation features of epitope residues and assessed the capacity of viral variant mutations to disrupt antibody recognition, revealing sets of antibodies predicted to effectively target recently described viral variants. This detailed structure-based reference of antibody RBD recognition signatures can inform therapeutic and vaccine design strategies.
format	article
author	Rui Yin Johnathan D Guest Ghazaleh Taherzadeh Ragul Gowthaman Ipsa Mittra Jane Quackenbush Brian G Pierce
author_facet	Rui Yin Johnathan D Guest Ghazaleh Taherzadeh Ragul Gowthaman Ipsa Mittra Jane Quackenbush Brian G Pierce
author_sort	Rui Yin
title	Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
title_short	Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
title_full	Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
title_fullStr	Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
title_full_unstemmed	Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.
title_sort	structural and energetic profiling of sars-cov-2 receptor binding domain antibody recognition and the impact of circulating variants.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/e124a4e516d34a9fbdf3e223838d242e
work_keys_str_mv	AT ruiyin structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT johnathandguest structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT ghazalehtaherzadeh structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT ragulgowthaman structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT ipsamittra structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT janequackenbush structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants AT briangpierce structuralandenergeticprofilingofsarscov2receptorbindingdomainantibodyrecognitionandtheimpactofcirculatingvariants
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Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants.

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