Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin

Abstract We present in this work a first X‐ray Absorption Spectroscopy study of the interactions of Zn with human BST2/tetherin and SARS‐CoV‐2 orf7a proteins as well as with some of their complexes. The analysis of the XANES region of the measured spectra shows that Zn binds to BST2, as well as to o...

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Autores principales:	Dr. Maria Petrosino, Dr. Francesco Stellato, Prof. Roberta Chiaraluce, Prof. Valerio Consalvi, Dr. Giovanni La Penna, Dr. Alessandra Pasquo, Dr. Olivier Proux, Prof. Giancarlo Rossi, Prof. Silvia Morante
Formato:	article
Lenguaje:	EN
Publicado:	Wiley-VCH 2021
Materias:	SARS-CoV-2 orf7a protein Tetherin/BST2 XANES Zn speciation Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/c57e1b68b9544cddb68fcd95f0b07719
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spelling	oai:doaj.org-article:c57e1b68b9544cddb68fcd95f0b077192021-11-27T06:12:47ZZn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin2191-136310.1002/open.202100217https://doaj.org/article/c57e1b68b9544cddb68fcd95f0b077192021-11-01T00:00:00Zhttps://doi.org/10.1002/open.202100217https://doaj.org/toc/2191-1363Abstract We present in this work a first X‐ray Absorption Spectroscopy study of the interactions of Zn with human BST2/tetherin and SARS‐CoV‐2 orf7a proteins as well as with some of their complexes. The analysis of the XANES region of the measured spectra shows that Zn binds to BST2, as well as to orf7a, thus resulting in the formation of BST2‐orf7a complexes. This structural information confirms the the conjecture, recently put forward by some of the present Authors, according to which the accessory orf7a (and possibly also orf8) viral protein are capable of interfering with the BST2 antiviral activity. Our explanation for this behavior is that, when BST2 gets in contact with Zn bound to the orf7a Cys15 ligand, it has the ability of displacing the metal owing to the creation of a new disulfide bridge across the two proteins. The formation of this BST2‐orf7a complex destabilizes BST2 dimerization, thus impairing the antiviral activity of the latter.Dr. Maria PetrosinoDr. Francesco StellatoProf. Roberta ChiaraluceProf. Valerio ConsalviDr. Giovanni La PennaDr. Alessandra PasquoDr. Olivier ProuxProf. Giancarlo RossiProf. Silvia MoranteWiley-VCHarticleSARS-CoV-2orf7a proteinTetherin/BST2XANESZn speciationChemistryQD1-999ENChemistryOpen, Vol 10, Iss 11, Pp 1133-1141 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	SARS-CoV-2 orf7a protein Tetherin/BST2 XANES Zn speciation Chemistry QD1-999
spellingShingle	SARS-CoV-2 orf7a protein Tetherin/BST2 XANES Zn speciation Chemistry QD1-999 Dr. Maria Petrosino Dr. Francesco Stellato Prof. Roberta Chiaraluce Prof. Valerio Consalvi Dr. Giovanni La Penna Dr. Alessandra Pasquo Dr. Olivier Proux Prof. Giancarlo Rossi Prof. Silvia Morante Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
description	Abstract We present in this work a first X‐ray Absorption Spectroscopy study of the interactions of Zn with human BST2/tetherin and SARS‐CoV‐2 orf7a proteins as well as with some of their complexes. The analysis of the XANES region of the measured spectra shows that Zn binds to BST2, as well as to orf7a, thus resulting in the formation of BST2‐orf7a complexes. This structural information confirms the the conjecture, recently put forward by some of the present Authors, according to which the accessory orf7a (and possibly also orf8) viral protein are capable of interfering with the BST2 antiviral activity. Our explanation for this behavior is that, when BST2 gets in contact with Zn bound to the orf7a Cys15 ligand, it has the ability of displacing the metal owing to the creation of a new disulfide bridge across the two proteins. The formation of this BST2‐orf7a complex destabilizes BST2 dimerization, thus impairing the antiviral activity of the latter.
format	article
author	Dr. Maria Petrosino Dr. Francesco Stellato Prof. Roberta Chiaraluce Prof. Valerio Consalvi Dr. Giovanni La Penna Dr. Alessandra Pasquo Dr. Olivier Proux Prof. Giancarlo Rossi Prof. Silvia Morante
author_facet	Dr. Maria Petrosino Dr. Francesco Stellato Prof. Roberta Chiaraluce Prof. Valerio Consalvi Dr. Giovanni La Penna Dr. Alessandra Pasquo Dr. Olivier Proux Prof. Giancarlo Rossi Prof. Silvia Morante
author_sort	Dr. Maria Petrosino
title	Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
title_short	Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
title_full	Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
title_fullStr	Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
title_full_unstemmed	Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin
title_sort	zn‐induced interactions between sars‐cov‐2 orf7a and bst2/tetherin
publisher	Wiley-VCH
publishDate	2021
url	https://doaj.org/article/c57e1b68b9544cddb68fcd95f0b07719
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Zn‐Induced Interactions Between SARS‐CoV‐2 orf7a and BST2/Tetherin

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