Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors

Abstract Several viruses of the corona family interact, via their spike (S) proteins, with human cellular receptors. Spike proteins of SARS-CoV-1 and SARS-CoV-2 virions, being structurally related but not identical, mediate attachment to the human angiotensin-converting enzyme 2 (hACE2) receptor in...

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Autores principales:	Jorge H. Rodriguez, Akshita Gupta
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/18044c32fd9a4bbc9757c788d956b9e8
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spelling	oai:doaj.org-article:18044c32fd9a4bbc9757c788d956b9e82021-12-02T14:12:09ZContact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors10.1038/s41598-020-80942-62045-2322https://doaj.org/article/18044c32fd9a4bbc9757c788d956b9e82021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-80942-6https://doaj.org/toc/2045-2322Abstract Several viruses of the corona family interact, via their spike (S) proteins, with human cellular receptors. Spike proteins of SARS-CoV-1 and SARS-CoV-2 virions, being structurally related but not identical, mediate attachment to the human angiotensin-converting enzyme 2 (hACE2) receptor in similar but non-identical ways. Molecular-level understanding of interactions between spike proteins and hACE2 can aid strategies for blocking attachment of SARS-CoV-1, a potentially reemerging health threat, to human cells. We have identified dominant molecular-level interactions, some attractive and some repulsive, between the receptor binding domain of SARS-CoV-1 spike proteins (S-RBD) and hACE2. We performed fragment-based quantum-biochemical calculations which directly relate biomolecular structure to the hACE2...S-RBD interaction energy. Consistent with X-ray crystallography and cryo-EM, the interaction energy between hACE2 and S-RBD ( $$\approx -$$ ≈ - 26 kcal/mol) corresponds to a net intermolecular attraction which is significantly enhanced by inclusion of dispersion van der Waals forces. Protein fragments at the hACE2...S-RBD interface, that dominate host-virus attraction, have been identified together with their constituent amino acid residues. Two hACE2 fragments which include residues (GLU37, ASP38, TYR41, GLN42) and (GLU329, LYS353, GLY354), respectively, as well as three S-RBD fragments which include residues (TYR436), (ARG426) and (THR487, GLY488, TYR491), respectively, have been identified as primary attractors at the hACE2...S-RBD interface.Jorge H. RodriguezAkshita GuptaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jorge H. Rodriguez Akshita Gupta Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
description	Abstract Several viruses of the corona family interact, via their spike (S) proteins, with human cellular receptors. Spike proteins of SARS-CoV-1 and SARS-CoV-2 virions, being structurally related but not identical, mediate attachment to the human angiotensin-converting enzyme 2 (hACE2) receptor in similar but non-identical ways. Molecular-level understanding of interactions between spike proteins and hACE2 can aid strategies for blocking attachment of SARS-CoV-1, a potentially reemerging health threat, to human cells. We have identified dominant molecular-level interactions, some attractive and some repulsive, between the receptor binding domain of SARS-CoV-1 spike proteins (S-RBD) and hACE2. We performed fragment-based quantum-biochemical calculations which directly relate biomolecular structure to the hACE2...S-RBD interaction energy. Consistent with X-ray crystallography and cryo-EM, the interaction energy between hACE2 and S-RBD ( $$\approx -$$ ≈ - 26 kcal/mol) corresponds to a net intermolecular attraction which is significantly enhanced by inclusion of dispersion van der Waals forces. Protein fragments at the hACE2...S-RBD interface, that dominate host-virus attraction, have been identified together with their constituent amino acid residues. Two hACE2 fragments which include residues (GLU37, ASP38, TYR41, GLN42) and (GLU329, LYS353, GLY354), respectively, as well as three S-RBD fragments which include residues (TYR436), (ARG426) and (THR487, GLY488, TYR491), respectively, have been identified as primary attractors at the hACE2...S-RBD interface.
format	article
author	Jorge H. Rodriguez Akshita Gupta
author_facet	Jorge H. Rodriguez Akshita Gupta
author_sort	Jorge H. Rodriguez
title	Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
title_short	Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
title_full	Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
title_fullStr	Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
title_full_unstemmed	Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors
title_sort	contact residue contributions to interaction energies between sars-cov-1 spike proteins and human ace2 receptors
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/18044c32fd9a4bbc9757c788d956b9e8
work_keys_str_mv	AT jorgehrodriguez contactresiduecontributionstointeractionenergiesbetweensarscov1spikeproteinsandhumanace2receptors AT akshitagupta contactresiduecontributionstointeractionenergiesbetweensarscov1spikeproteinsandhumanace2receptors
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Contact residue contributions to interaction energies between SARS-CoV-1 spike proteins and human ACE2 receptors

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