Author: Morsy, Sara; Morsy, Ahmed
Title: Epitope mimicry analysis of SARS-COV-2 surface proteins and human lung proteins Cord-id: feff1hn6 Document date: 2021_2_4
ID: feff1hn6
Snippet: BACKGROUND: Autoimmune response after the infection of SARS-COV-2 is evident as more cases of Guillain Barre syndrome and Kawasaki disease are diagnosed after infection. In this study, we aim to investigate a possible mechanism of autoimmune lung injury. METHODS: We extracted the peptide sequence surface proteins of the SARS-COV-2 from NCBI data protein. We used Blastp to assess the homologous sequences between the human protein in the UNIPROT database that is associated with respiratory distres
Document: BACKGROUND: Autoimmune response after the infection of SARS-COV-2 is evident as more cases of Guillain Barre syndrome and Kawasaki disease are diagnosed after infection. In this study, we aim to investigate a possible mechanism of autoimmune lung injury. METHODS: We extracted the peptide sequence surface proteins of the SARS-COV-2 from NCBI data protein. We used Blastp to assess the homologous sequences between the human protein in the UNIPROT database that is 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, MHC-II and B-cell epitope 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.
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