Tau protein aggregation associated with SARS-CoV-2 main protease
The primary function of virus proteases is the proteolytic processing of the viral polyprotein. These enzymes can also cleave host cell proteins, which is important for viral pathogenicity, modulation of cellular processes, viral replication, the defeat of antiviral responses and modulation of the i...
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| creator | Eberle, Raphael Josef Coronado, Mônika Aparecida Gering, Ian Sommerhage, Simon Korostov, Karolina Stefanski, Anja Stühler, Kai Kraemer-Schulien, Victoria Blömeke, Lara Bannach, Oliver Willbold, Dieter |
| description | The primary function of virus proteases is the proteolytic processing of the viral polyprotein. These enzymes can also cleave host cell proteins, which is important for viral pathogenicity, modulation of cellular processes, viral replication, the defeat of antiviral responses and modulation of the immune response. It is known that COVID-19 can influence multiple tissues or organs and that infection can damage the functionality of the brain in multiple ways. After COVID-19 infections, amyloid-[beta], neurogranin, tau and phosphorylated tau were detected extracellularly, implicating possible neurodegenerative processes. The present study describes the possible induction of tau aggregation by the SARS-CoV-2 3CL protease (3CL.sup.pro) possibly relevant in neuropathology. Further investigations demonstrated that tau was proteolytically cleaved by the viral protease 3CL and, consequently, generated aggregates. However, more evidence is needed to confirm that COVID-19 is able to trigger neurodegenerative diseases. |
| doi_str_mv | 10.1371/journal.pone.0288138 |
| format | Article |
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These enzymes can also cleave host cell proteins, which is important for viral pathogenicity, modulation of cellular processes, viral replication, the defeat of antiviral responses and modulation of the immune response. It is known that COVID-19 can influence multiple tissues or organs and that infection can damage the functionality of the brain in multiple ways. After COVID-19 infections, amyloid-[beta], neurogranin, tau and phosphorylated tau were detected extracellularly, implicating possible neurodegenerative processes. The present study describes the possible induction of tau aggregation by the SARS-CoV-2 3CL protease (3CL.sup.pro) possibly relevant in neuropathology. Further investigations demonstrated that tau was proteolytically cleaved by the viral protease 3CL and, consequently, generated aggregates. However, more evidence is needed to confirm that COVID-19 is able to trigger neurodegenerative diseases.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0288138</identifier><identifier>PMID: 37603556</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Alzheimer's disease ; Analysis ; Antibodies ; Anticoagulants ; Antiviral agents ; Biology and life sciences ; Brain damage ; Cloning ; COVID-19 ; Enzymes ; Ethylenediaminetetraacetic acid ; Experiments ; Health aspects ; Immune response ; Immunomodulation ; Infection ; Infections ; Instrument industry ; Medicine and health sciences ; Modulation ; Nervous system diseases ; Neurodegeneration ; Neurodegenerative diseases ; Neurogranin ; Pathogenicity ; Pathogens ; Physical Sciences ; Protease ; Proteases ; Protein interaction ; Proteinase ; Proteins ; Proteolysis ; Research and analysis methods ; Scientific equipment and supplies industry ; Severe acute respiratory syndrome coronavirus 2 ; Tau protein ; Tau proteins ; Viral diseases ; Viruses ; β-Amyloid</subject><ispartof>PloS one, 2023-08, Vol.18 (8), p.e0288138-e0288138</ispartof><rights>COPYRIGHT 2023 Public Library of Science</rights><rights>2023 Eberle et al. 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| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2023-08, Vol.18 (8), p.e0288138-e0288138 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_2854333308 |
| source | DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Alzheimer's disease Analysis Antibodies Anticoagulants Antiviral agents Biology and life sciences Brain damage Cloning COVID-19 Enzymes Ethylenediaminetetraacetic acid Experiments Health aspects Immune response Immunomodulation Infection Infections Instrument industry Medicine and health sciences Modulation Nervous system diseases Neurodegeneration Neurodegenerative diseases Neurogranin Pathogenicity Pathogens Physical Sciences Protease Proteases Protein interaction Proteinase Proteins Proteolysis Research and analysis methods Scientific equipment and supplies industry Severe acute respiratory syndrome coronavirus 2 Tau protein Tau proteins Viral diseases Viruses β-Amyloid |
| title | Tau protein aggregation associated with SARS-CoV-2 main protease |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T03%3A32%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tau%20protein%20aggregation%20associated%20with%20SARS-CoV-2%20main%20protease&rft.jtitle=PloS%20one&rft.au=Eberle,%20Raphael%20Josef&rft.date=2023-08-21&rft.volume=18&rft.issue=8&rft.spage=e0288138&rft.epage=e0288138&rft.pages=e0288138-e0288138&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0288138&rft_dat=%3Cgale_plos_%3EA761643499%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2854333308&rft_id=info:pmid/37603556&rft_galeid=A761643499&rft_doaj_id=oai_doaj_org_article_4b1a1dc1a93a4cafb63cb4de6badfe8e&rfr_iscdi=true |