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.

Zn-induced interactions between SARS-CoV-2 orf7a and BST2/Tetherin / Petrosino, Maria; Stellato, Francesco; Chiaraluce, Roberta; Consalvi, Valerio; La Penna, Giovanni; Pasquo, Alessandra; Proux, Olivier; Rossi, Giancarlo; Morante, Silvia. - In: CHEMISTRYOPEN. - ISSN 2191-1363. - 10:11(2021), pp. 1133-1141. [10.1002/open.202100217]

Zn-induced interactions between SARS-CoV-2 orf7a and BST2/Tetherin

Petrosino, Maria
Co-primo
;
Chiaraluce, Roberta;Consalvi, Valerio;
2021

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.
2021
orf7a protein; SARS-CoV-2; Tetherin/BST2; XANES; Zn speciation; Antigens, CD; Cysteine; GPI-Linked Proteins; Histidine; Humans; Molecular Dynamics Simulation; Protein Binding; SARS-CoV-2; Viral Proteins; X-Ray Absorption Spectroscopy; Zinc
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Zn-induced interactions between SARS-CoV-2 orf7a and BST2/Tetherin / Petrosino, Maria; Stellato, Francesco; Chiaraluce, Roberta; Consalvi, Valerio; La Penna, Giovanni; Pasquo, Alessandra; Proux, Olivier; Rossi, Giancarlo; Morante, Silvia. - In: CHEMISTRYOPEN. - ISSN 2191-1363. - 10:11(2021), pp. 1133-1141. [10.1002/open.202100217]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1586113
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