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Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication

In SARS-CoV-2, at the S1/S2 furin cleavage site, a four amino acid insert (P-R-R-A) not found in closely related corona viruses, has been shown to facilitate entry into respiratory epithelial cells and promote virus transmission, infectivity and virulence. By cupric aerosol treatment, complexation o...

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Autores principales: Deloncle, Roger, Guillard, Olivier, Pineau, Alain, Lesage, Gérard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Author(s). Published by Elsevier Ltd. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8788156/
https://www.ncbi.nlm.nih.gov/pubmed/35095175
http://dx.doi.org/10.1016/j.mehy.2022.110775
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author Deloncle, Roger
Guillard, Olivier
Pineau, Alain
Lesage, Gérard
author_facet Deloncle, Roger
Guillard, Olivier
Pineau, Alain
Lesage, Gérard
author_sort Deloncle, Roger
collection PubMed
description In SARS-CoV-2, at the S1/S2 furin cleavage site, a four amino acid insert (P-R-R-A) not found in closely related corona viruses, has been shown to facilitate entry into respiratory epithelial cells and promote virus transmission, infectivity and virulence. By cupric aerosol treatment, complexation of these four amino acids (-P-R-R-A-), at the spike (S) protein site will lead to a conformational change possibly impeding SARS-CoV-2 replication process in the respiratory track. Since these four amino acids yield strong and stable copper complexes, subsequent to a steric hindrance, this complexation will disturb the furin-like protease cleavage at the spike protein site as it has been recently shown in vitro with copper gluconate. The compilation of stability constants for copper amino-acid complex formation, showing values of the same order of magnitude for all the twenty proteinogenic amino-acids demonstrate thermodynamically that copper amino-acid chelation for SARS-CoV-2 virus will not be affected by mutations leading to amino acid exchanges in the spike protein region. Given its low toxicity, and its very low stability formation constant, copper acetate is proposed rather than copper gluconate for possible cupric aerosol or nasal spray treatments aimed at impeding SARS-CoV-2 multiplication. It will open different medical perspectives, complementary to vaccination, in the fight against COVID 19 native virus, variants and future mutants.
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spelling pubmed-87881562022-01-25 Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication Deloncle, Roger Guillard, Olivier Pineau, Alain Lesage, Gérard Med Hypotheses Article In SARS-CoV-2, at the S1/S2 furin cleavage site, a four amino acid insert (P-R-R-A) not found in closely related corona viruses, has been shown to facilitate entry into respiratory epithelial cells and promote virus transmission, infectivity and virulence. By cupric aerosol treatment, complexation of these four amino acids (-P-R-R-A-), at the spike (S) protein site will lead to a conformational change possibly impeding SARS-CoV-2 replication process in the respiratory track. Since these four amino acids yield strong and stable copper complexes, subsequent to a steric hindrance, this complexation will disturb the furin-like protease cleavage at the spike protein site as it has been recently shown in vitro with copper gluconate. The compilation of stability constants for copper amino-acid complex formation, showing values of the same order of magnitude for all the twenty proteinogenic amino-acids demonstrate thermodynamically that copper amino-acid chelation for SARS-CoV-2 virus will not be affected by mutations leading to amino acid exchanges in the spike protein region. Given its low toxicity, and its very low stability formation constant, copper acetate is proposed rather than copper gluconate for possible cupric aerosol or nasal spray treatments aimed at impeding SARS-CoV-2 multiplication. It will open different medical perspectives, complementary to vaccination, in the fight against COVID 19 native virus, variants and future mutants. The Author(s). Published by Elsevier Ltd. 2022-03 2022-01-25 /pmc/articles/PMC8788156/ /pubmed/35095175 http://dx.doi.org/10.1016/j.mehy.2022.110775 Text en © 2022 The Author(s) Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Deloncle, Roger
Guillard, Olivier
Pineau, Alain
Lesage, Gérard
Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title_full Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title_fullStr Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title_full_unstemmed Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title_short Copper acetate aerosols: A possible tool complementary to vaccination in fight against SARS-CoV-2 and variants replication
title_sort copper acetate aerosols: a possible tool complementary to vaccination in fight against sars-cov-2 and variants replication
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8788156/
https://www.ncbi.nlm.nih.gov/pubmed/35095175
http://dx.doi.org/10.1016/j.mehy.2022.110775
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