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Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins
BACKGROUND: Autoimmune response after the infection of SARS-COV-2 is evident as more cases of Guillain Barre syndrome and Kawasaki disease are diagnosed. In this study, we aim to investigate a possible mechanism of autoimmune lung injury. METHODS: We extracted the peptide sequences of surface protei...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859657/ https://www.ncbi.nlm.nih.gov/pubmed/33588349 http://dx.doi.org/10.1016/j.jmgm.2021.107836 |
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author | Morsy, Sara Morsy, Ahmed |
author_facet | Morsy, Sara Morsy, Ahmed |
author_sort | Morsy, Sara |
collection | PubMed |
description | BACKGROUND: Autoimmune response after the infection of SARS-COV-2 is evident as more cases of Guillain Barre syndrome and Kawasaki disease are diagnosed. In this study, we aim to investigate a possible mechanism of autoimmune lung injury. METHODS: We extracted the peptide sequences of surface proteins of the SARS-COV-2 from the NCBI data protein. We used Blastp to assess the homologous sequences between the human proteins in the UNIPROT database that are associated with respiratory distress. Then, we filtered the homologous sequences to those selectively expressed in the lung and homologous to surface viral proteins. We then assessed the epitope sequences for MHC-I and MHC-II using recommended settings and reference MHC in the IEDB database. RESULTS: Homeobox protein 2.1 (NKX2-1) and ATP-binding cassette sub-family A member 3 (ABCA3) showed homologous sequence to both surface glycoproteins and envelope proteins. The HLA-DR and HLA-DQ had a similar binding pattern to ABCA3 as surface glycoproteins and envelope proteins, respectively. Other HLA molecules that had a similar binding pattern to SARS-COV-2 as human proteins were HLA-A and HLA-DP. CONCLUSION: Our study indicates that there is a possible autoimmune mechanism underlying the acute respiratory distress syndrome in SARS-COV-2. |
format | Online Article Text |
id | pubmed-7859657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-78596572021-02-04 Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins Morsy, Sara Morsy, Ahmed J Mol Graph Model Article BACKGROUND: Autoimmune response after the infection of SARS-COV-2 is evident as more cases of Guillain Barre syndrome and Kawasaki disease are diagnosed. In this study, we aim to investigate a possible mechanism of autoimmune lung injury. METHODS: We extracted the peptide sequences of surface proteins of the SARS-COV-2 from the NCBI data protein. We used Blastp to assess the homologous sequences between the human proteins in the UNIPROT database that are associated with respiratory distress. Then, we filtered the homologous sequences to those selectively expressed in the lung and homologous to surface viral proteins. We then assessed the epitope sequences for MHC-I and MHC-II using recommended settings and reference MHC in the IEDB database. RESULTS: Homeobox protein 2.1 (NKX2-1) and ATP-binding cassette sub-family A member 3 (ABCA3) showed homologous sequence to both surface glycoproteins and envelope proteins. The HLA-DR and HLA-DQ had a similar binding pattern to ABCA3 as surface glycoproteins and envelope proteins, respectively. Other HLA molecules that had a similar binding pattern to SARS-COV-2 as human proteins were HLA-A and HLA-DP. CONCLUSION: Our study indicates that there is a possible autoimmune mechanism underlying the acute respiratory distress syndrome in SARS-COV-2. Elsevier Inc. 2021-06 2021-02-04 /pmc/articles/PMC7859657/ /pubmed/33588349 http://dx.doi.org/10.1016/j.jmgm.2021.107836 Text en © 2021 Elsevier Inc. All rights reserved. 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 Morsy, Sara Morsy, Ahmed Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title | Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title_full | Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title_fullStr | Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title_full_unstemmed | Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title_short | Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins |
title_sort | epitope mimicry analysis of sars-cov-2 surface proteins and human lung proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7859657/ https://www.ncbi.nlm.nih.gov/pubmed/33588349 http://dx.doi.org/10.1016/j.jmgm.2021.107836 |
work_keys_str_mv | AT morsysara epitopemimicryanalysisofsarscov2surfaceproteinsandhumanlungproteins AT morsyahmed epitopemimicryanalysisofsarscov2surfaceproteinsandhumanlungproteins |