Identification of Human Host Substrates of the SARS-CoV-2 M pro and PL pro Using Subtiligase N-Terminomics
The recent emergence of SARS-CoV-2 in the human population has caused a global pandemic. The virus encodes two proteases, M and PL , that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substr...
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| Veröffentlicht in: | ACS infectious diseases 2023-04, Vol.9 (4), p.749-761 |
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| creator | Luo, Shu Y Moussa, Eman W Lopez-Orozco, Joaquin Felix-Lopez, Alberto Ishida, Ray Fayad, Nawell Gomez-Cardona, Erik Wang, Henry Wilson, Joyce A Kumar, Anil Hobman, Tom C Julien, Olivier |
| description | The recent emergence of SARS-CoV-2 in the human population has caused a global pandemic. The virus encodes two proteases, M
and PL
, that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substrates of these proteases, active recombinant SARS-CoV-2 M
and PL
were added to A549 and Jurkat human cell lysates, and subtiligase-mediated N-terminomics was used to capture and enrich protease substrate fragments. The precise location of each cleavage site was identified using mass spectrometry. Here, we report the identification of over 200 human host proteins that are potential substrates for SARS-CoV-2 M
and PL
and provide a global mapping of proteolysis for these two viral proteases in vitro. Modulating proteolysis of these substrates will increase our understanding of SARS-CoV-2 pathobiology and COVID-19. |
| doi_str_mv | 10.1021/acsinfecdis.2c00458 |
| format | Article |
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and PL
, that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substrates of these proteases, active recombinant SARS-CoV-2 M
and PL
were added to A549 and Jurkat human cell lysates, and subtiligase-mediated N-terminomics was used to capture and enrich protease substrate fragments. The precise location of each cleavage site was identified using mass spectrometry. Here, we report the identification of over 200 human host proteins that are potential substrates for SARS-CoV-2 M
and PL
and provide a global mapping of proteolysis for these two viral proteases in vitro. Modulating proteolysis of these substrates will increase our understanding of SARS-CoV-2 pathobiology and COVID-19.</description><identifier>ISSN: 2373-8227</identifier><identifier>EISSN: 2373-8227</identifier><identifier>DOI: 10.1021/acsinfecdis.2c00458</identifier><identifier>PMID: 37011043</identifier><language>eng</language><publisher>United States</publisher><subject>COVID-19 ; Humans ; Peptide Hydrolases - metabolism ; Peptide Synthases ; SARS-CoV-2 - metabolism</subject><ispartof>ACS infectious diseases, 2023-04, Vol.9 (4), p.749-761</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1173-22994df6a6eb3481cb40fdb25e39bb9639a3d2c0353cc38c4438fbaae8819f583</citedby><cites>FETCH-LOGICAL-c1173-22994df6a6eb3481cb40fdb25e39bb9639a3d2c0353cc38c4438fbaae8819f583</cites><orcidid>0000-0001-7068-7299 ; 0000-0002-5730-1571 ; 0000-0002-6179-4516</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2765,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37011043$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Luo, Shu Y</creatorcontrib><creatorcontrib>Moussa, Eman W</creatorcontrib><creatorcontrib>Lopez-Orozco, Joaquin</creatorcontrib><creatorcontrib>Felix-Lopez, Alberto</creatorcontrib><creatorcontrib>Ishida, Ray</creatorcontrib><creatorcontrib>Fayad, Nawell</creatorcontrib><creatorcontrib>Gomez-Cardona, Erik</creatorcontrib><creatorcontrib>Wang, Henry</creatorcontrib><creatorcontrib>Wilson, Joyce A</creatorcontrib><creatorcontrib>Kumar, Anil</creatorcontrib><creatorcontrib>Hobman, Tom C</creatorcontrib><creatorcontrib>Julien, Olivier</creatorcontrib><title>Identification of Human Host Substrates of the SARS-CoV-2 M pro and PL pro Using Subtiligase N-Terminomics</title><title>ACS infectious diseases</title><addtitle>ACS Infect Dis</addtitle><description>The recent emergence of SARS-CoV-2 in the human population has caused a global pandemic. The virus encodes two proteases, M
and PL
, that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substrates of these proteases, active recombinant SARS-CoV-2 M
and PL
were added to A549 and Jurkat human cell lysates, and subtiligase-mediated N-terminomics was used to capture and enrich protease substrate fragments. The precise location of each cleavage site was identified using mass spectrometry. Here, we report the identification of over 200 human host proteins that are potential substrates for SARS-CoV-2 M
and PL
and provide a global mapping of proteolysis for these two viral proteases in vitro. Modulating proteolysis of these substrates will increase our understanding of SARS-CoV-2 pathobiology and COVID-19.</description><subject>COVID-19</subject><subject>Humans</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Peptide Synthases</subject><subject>SARS-CoV-2 - metabolism</subject><issn>2373-8227</issn><issn>2373-8227</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkNtqAjEQhkNpqWJ9gkLJC6xNMlnNXoq0VbAHqvZ2ydFG3F1J4oVv37Xa4tX8MHzDPx9C95QMKGH0Ueroa2e18XHANCE8F1eoy2AEmWBsdH2RO6gf44YQQkHknOe3qAMjQinh0EWbmbF18s5rmXxT48bh6b6SNZ42MeHFXsUUZLLxuEjfFi_Gn4ts0nxlDL_iXWiwrA3-mP_GVVtpfWSS3_q1jBa_ZUsbKl83ldfxDt04uY22f549tHp-Wk6m2fz9ZTYZzzNNaVuZsaLgxg3l0CrggmrFiTOK5RYKpYohFBJM-zLkoDUIzTkIp6S0QtDC5QJ6CE53dWhiDNaVu-ArGQ4lJeVRXnkhrzzLa6mHE7Xbq8qaf-ZPFfwAKhBtSg</recordid><startdate>20230414</startdate><enddate>20230414</enddate><creator>Luo, Shu Y</creator><creator>Moussa, Eman W</creator><creator>Lopez-Orozco, Joaquin</creator><creator>Felix-Lopez, Alberto</creator><creator>Ishida, Ray</creator><creator>Fayad, Nawell</creator><creator>Gomez-Cardona, Erik</creator><creator>Wang, Henry</creator><creator>Wilson, Joyce A</creator><creator>Kumar, Anil</creator><creator>Hobman, Tom C</creator><creator>Julien, Olivier</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0001-7068-7299</orcidid><orcidid>https://orcid.org/0000-0002-5730-1571</orcidid><orcidid>https://orcid.org/0000-0002-6179-4516</orcidid></search><sort><creationdate>20230414</creationdate><title>Identification of Human Host Substrates of the SARS-CoV-2 M pro and PL pro Using Subtiligase N-Terminomics</title><author>Luo, Shu Y ; Moussa, Eman W ; Lopez-Orozco, Joaquin ; Felix-Lopez, Alberto ; Ishida, Ray ; Fayad, Nawell ; Gomez-Cardona, Erik ; Wang, Henry ; Wilson, Joyce A ; Kumar, Anil ; Hobman, Tom C ; Julien, Olivier</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1173-22994df6a6eb3481cb40fdb25e39bb9639a3d2c0353cc38c4438fbaae8819f583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>COVID-19</topic><topic>Humans</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Peptide Synthases</topic><topic>SARS-CoV-2 - metabolism</topic><toplevel>online_resources</toplevel><creatorcontrib>Luo, Shu Y</creatorcontrib><creatorcontrib>Moussa, Eman W</creatorcontrib><creatorcontrib>Lopez-Orozco, Joaquin</creatorcontrib><creatorcontrib>Felix-Lopez, Alberto</creatorcontrib><creatorcontrib>Ishida, Ray</creatorcontrib><creatorcontrib>Fayad, Nawell</creatorcontrib><creatorcontrib>Gomez-Cardona, Erik</creatorcontrib><creatorcontrib>Wang, Henry</creatorcontrib><creatorcontrib>Wilson, Joyce A</creatorcontrib><creatorcontrib>Kumar, Anil</creatorcontrib><creatorcontrib>Hobman, Tom C</creatorcontrib><creatorcontrib>Julien, Olivier</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>ACS infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Luo, Shu Y</au><au>Moussa, Eman W</au><au>Lopez-Orozco, Joaquin</au><au>Felix-Lopez, Alberto</au><au>Ishida, Ray</au><au>Fayad, Nawell</au><au>Gomez-Cardona, Erik</au><au>Wang, Henry</au><au>Wilson, Joyce A</au><au>Kumar, Anil</au><au>Hobman, Tom C</au><au>Julien, Olivier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Human Host Substrates of the SARS-CoV-2 M pro and PL pro Using Subtiligase N-Terminomics</atitle><jtitle>ACS infectious diseases</jtitle><addtitle>ACS Infect Dis</addtitle><date>2023-04-14</date><risdate>2023</risdate><volume>9</volume><issue>4</issue><spage>749</spage><epage>761</epage><pages>749-761</pages><issn>2373-8227</issn><eissn>2373-8227</eissn><abstract>The recent emergence of SARS-CoV-2 in the human population has caused a global pandemic. The virus encodes two proteases, M
and PL
, that are thought to play key roles in the suppression of host protein synthesis and immune response evasion during infection. To identify the specific host cell substrates of these proteases, active recombinant SARS-CoV-2 M
and PL
were added to A549 and Jurkat human cell lysates, and subtiligase-mediated N-terminomics was used to capture and enrich protease substrate fragments. The precise location of each cleavage site was identified using mass spectrometry. Here, we report the identification of over 200 human host proteins that are potential substrates for SARS-CoV-2 M
and PL
and provide a global mapping of proteolysis for these two viral proteases in vitro. Modulating proteolysis of these substrates will increase our understanding of SARS-CoV-2 pathobiology and COVID-19.</abstract><cop>United States</cop><pmid>37011043</pmid><doi>10.1021/acsinfecdis.2c00458</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0001-7068-7299</orcidid><orcidid>https://orcid.org/0000-0002-5730-1571</orcidid><orcidid>https://orcid.org/0000-0002-6179-4516</orcidid></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | COVID-19 Humans Peptide Hydrolases - metabolism Peptide Synthases SARS-CoV-2 - metabolism |
| title | Identification of Human Host Substrates of the SARS-CoV-2 M pro and PL pro Using Subtiligase N-Terminomics |
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