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Homology between SARS CoV-2 and human proteins
An extremely high contagiousness of SARS CoV-2 indicates that the virus developed the ability to deceive the innate immune system. The virus could have included in its outer protein domains some motifs that are structurally similar to those that the potential victim's immune system has learned...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8387358/ https://www.ncbi.nlm.nih.gov/pubmed/34433832 http://dx.doi.org/10.1038/s41598-021-96233-7 |
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author | Khavinson, Vladimir Terekhov, Alexander Kormilets, Dmitry Maryanovich, Alexander |
author_facet | Khavinson, Vladimir Terekhov, Alexander Kormilets, Dmitry Maryanovich, Alexander |
author_sort | Khavinson, Vladimir |
collection | PubMed |
description | An extremely high contagiousness of SARS CoV-2 indicates that the virus developed the ability to deceive the innate immune system. The virus could have included in its outer protein domains some motifs that are structurally similar to those that the potential victim's immune system has learned to ignore. The similarity of the primary structures of the viral and human proteins can provoke an autoimmune process. Using an open-access protein database Uniprot, we have compared the SARS CoV-2 proteome with those of other organisms. In the SARS CoV-2 spike (S) protein molecule, we have localized more than two dozen hepta- and octamers homologous to human proteins. They are scattered along the entire length of the S protein molecule, while some of them fuse into sequences of considerable length. Except for one, all these n-mers project from the virus particle and therefore can be involved in providing mimicry and misleading the immune system. All hepta- and octamers of the envelope (E) protein, homologous to human proteins, are located in the viral transmembrane domain and form a 28-mer protein E(14-41) VNSVLLFLAFVVFLLVTLAILTALRLCA. The involvement of the protein E in provoking an autoimmune response (after the destruction of the virus particle) seems to be highly likely. Some SARS CoV-2 nonstructural proteins may also be involved in this process, namely ORF3a, ORF7a, ORF7b, ORF8, and ORF9b. It is possible that ORF7b is involved in the dysfunction of olfactory receptors, and the S protein in the dysfunction of taste perception. |
format | Online Article Text |
id | pubmed-8387358 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-83873582021-09-01 Homology between SARS CoV-2 and human proteins Khavinson, Vladimir Terekhov, Alexander Kormilets, Dmitry Maryanovich, Alexander Sci Rep Article An extremely high contagiousness of SARS CoV-2 indicates that the virus developed the ability to deceive the innate immune system. The virus could have included in its outer protein domains some motifs that are structurally similar to those that the potential victim's immune system has learned to ignore. The similarity of the primary structures of the viral and human proteins can provoke an autoimmune process. Using an open-access protein database Uniprot, we have compared the SARS CoV-2 proteome with those of other organisms. In the SARS CoV-2 spike (S) protein molecule, we have localized more than two dozen hepta- and octamers homologous to human proteins. They are scattered along the entire length of the S protein molecule, while some of them fuse into sequences of considerable length. Except for one, all these n-mers project from the virus particle and therefore can be involved in providing mimicry and misleading the immune system. All hepta- and octamers of the envelope (E) protein, homologous to human proteins, are located in the viral transmembrane domain and form a 28-mer protein E(14-41) VNSVLLFLAFVVFLLVTLAILTALRLCA. The involvement of the protein E in provoking an autoimmune response (after the destruction of the virus particle) seems to be highly likely. Some SARS CoV-2 nonstructural proteins may also be involved in this process, namely ORF3a, ORF7a, ORF7b, ORF8, and ORF9b. It is possible that ORF7b is involved in the dysfunction of olfactory receptors, and the S protein in the dysfunction of taste perception. Nature Publishing Group UK 2021-08-25 /pmc/articles/PMC8387358/ /pubmed/34433832 http://dx.doi.org/10.1038/s41598-021-96233-7 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Khavinson, Vladimir Terekhov, Alexander Kormilets, Dmitry Maryanovich, Alexander Homology between SARS CoV-2 and human proteins |
title | Homology between SARS CoV-2 and human proteins |
title_full | Homology between SARS CoV-2 and human proteins |
title_fullStr | Homology between SARS CoV-2 and human proteins |
title_full_unstemmed | Homology between SARS CoV-2 and human proteins |
title_short | Homology between SARS CoV-2 and human proteins |
title_sort | homology between sars cov-2 and human proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8387358/ https://www.ncbi.nlm.nih.gov/pubmed/34433832 http://dx.doi.org/10.1038/s41598-021-96233-7 |
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