Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19
Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, t...
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| Veröffentlicht in: | Cell stress & chaperones 2020-09, Vol.25 (5), p.737-741 |
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| creator | Gammazza, Antonella Marino Légaré, Sébastien Lo Bosco, Giosuè Fucarino, Alberto Angileri, Francesca de Macario, Everly Conway Macario, Alberto JL Cappello, Francesco |
| description | Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endothelial cell plasma-cell membrane localization has already been demonstrated. We also postulate that post-translational modifications, induced by physical (shear) and chemical (metabolic) stress caused respectively by the risk factors hypertension and diabetes, might have a role in determining plasma-cell membrane localization and, in turn, autoimmune-induced endothelial damage. |
| doi_str_mv | 10.1007/s12192-020-01148-3 |
| format | Article |
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We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endothelial cell plasma-cell membrane localization has already been demonstrated. We also postulate that post-translational modifications, induced by physical (shear) and chemical (metabolic) stress caused respectively by the risk factors hypertension and diabetes, might have a role in determining plasma-cell membrane localization and, in turn, autoimmune-induced endothelial damage.</description><identifier>ISSN: 1355-8145</identifier><identifier>EISSN: 1466-1268</identifier><identifier>DOI: 10.1007/s12192-020-01148-3</identifier><identifier>PMID: 32754823</identifier><language>eng</language><publisher>Dordrecht: Springer Science + Business Media</publisher><subject>Amino Acid Sequence ; Amino acids ; Antibodies ; Antigens ; Autoantigens ; Autoimmune diseases ; Autoimmunity ; Betacoronavirus - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Cell Biology ; Cell membranes ; Chaperones ; Coronavirus Infections - virology ; Coronaviruses ; COVID-19 ; Damage localization ; Databases, Protein ; Diabetes mellitus ; Effector cells ; Endothelial cells ; Endothelial Cells - metabolism ; Epitopes ; Health risks ; Heat shock proteins ; Heat-Shock Proteins - chemistry ; Heat-Shock Proteins - immunology ; Humans ; Hypertension ; Immune system ; Immunodominant Epitopes ; Immunogenicity ; Immunology ; Life Sciences & Biomedicine ; Localization ; Mimicry ; Molecular Mimicry ; Neurosciences ; Pandemics ; Pneumonia, Viral - virology ; Post-translation ; Proteins ; Risk analysis ; Risk factors ; SARS-CoV-2 ; Science & Technology ; Severe acute respiratory syndrome ; Severe acute respiratory syndrome coronavirus 2 ; SHORT COMMUNICATION ; Viral diseases ; Viral Proteins - chemistry ; Viral Proteins - immunology ; Viruses</subject><ispartof>Cell stress & chaperones, 2020-09, Vol.25 (5), p.737-741</ispartof><rights>Cell Stress Society International 2020</rights><rights>Cell Stress Society International 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>79</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000555742800001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c496t-488636eb9f5f21ffa5f30dd26401ff48d5481981bf6e1300b9d6b4b7a4bc381b3</citedby><cites>FETCH-LOGICAL-c496t-488636eb9f5f21ffa5f30dd26401ff48d5481981bf6e1300b9d6b4b7a4bc381b3</cites><orcidid>0000-0001-9288-1148 ; 0000-0002-1602-0693 ; 0000-0001-8958-525X ; 0000-0002-7993-6965</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/48724236$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/48724236$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27929,27930,28253,41493,42562,51324,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32754823$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gammazza, Antonella Marino</creatorcontrib><creatorcontrib>Légaré, Sébastien</creatorcontrib><creatorcontrib>Lo Bosco, Giosuè</creatorcontrib><creatorcontrib>Fucarino, Alberto</creatorcontrib><creatorcontrib>Angileri, Francesca</creatorcontrib><creatorcontrib>de Macario, Everly Conway</creatorcontrib><creatorcontrib>Macario, Alberto JL</creatorcontrib><creatorcontrib>Cappello, Francesco</creatorcontrib><title>Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19</title><title>Cell stress & chaperones</title><addtitle>Cell Stress and Chaperones</addtitle><addtitle>CELL STRESS CHAPERON</addtitle><addtitle>Cell Stress Chaperones</addtitle><description>Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endothelial cell plasma-cell membrane localization has already been demonstrated. We also postulate that post-translational modifications, induced by physical (shear) and chemical (metabolic) stress caused respectively by the risk factors hypertension and diabetes, might have a role in determining plasma-cell membrane localization and, in turn, autoimmune-induced endothelial damage.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Autoantigens</subject><subject>Autoimmune diseases</subject><subject>Autoimmunity</subject><subject>Betacoronavirus - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell membranes</subject><subject>Chaperones</subject><subject>Coronavirus Infections - virology</subject><subject>Coronaviruses</subject><subject>COVID-19</subject><subject>Damage localization</subject><subject>Databases, Protein</subject><subject>Diabetes mellitus</subject><subject>Effector cells</subject><subject>Endothelial cells</subject><subject>Endothelial Cells - 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We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endothelial cell plasma-cell membrane localization has already been demonstrated. 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| subjects | Amino Acid Sequence Amino acids Antibodies Antigens Autoantigens Autoimmune diseases Autoimmunity Betacoronavirus - metabolism Biochemistry Biomedical and Life Sciences Biomedicine Cancer Research Cell Biology Cell membranes Chaperones Coronavirus Infections - virology Coronaviruses COVID-19 Damage localization Databases, Protein Diabetes mellitus Effector cells Endothelial cells Endothelial Cells - metabolism Epitopes Health risks Heat shock proteins Heat-Shock Proteins - chemistry Heat-Shock Proteins - immunology Humans Hypertension Immune system Immunodominant Epitopes Immunogenicity Immunology Life Sciences & Biomedicine Localization Mimicry Molecular Mimicry Neurosciences Pandemics Pneumonia, Viral - virology Post-translation Proteins Risk analysis Risk factors SARS-CoV-2 Science & Technology Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 SHORT COMMUNICATION Viral diseases Viral Proteins - chemistry Viral Proteins - immunology Viruses |
| title | Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19 |
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