Activity‐based proteomics reveals nine target proteases for the recombinant protein‐stabilizing inhibitor SlCYS8 in Nicotiana benthamiana
Summary Co‐expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity‐based protein profiling to identify proteases that are inhibit...
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| Veröffentlicht in: | Plant biotechnology journal 2019-08, Vol.17 (8), p.1670-1678 |
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| creator | Jutras, Philippe V. Grosse‐Holz, Friederike Kaschani, Farnusch Kaiser, Markus Michaud, Dominique Hoorn, Renier A.L. |
| description | Summary
Co‐expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity‐based protein profiling to identify proteases that are inhibited by SlCYS8 in agroinfiltrated Nicotiana benthamiana. We discovered that SlCYS8 selectively suppresses papain‐like cysteine protease (PLCP) activity in both apoplastic fluids and total leaf extracts, while not affecting vacuolar‐processing enzyme and serine hydrolase activity. A robust concentration‐dependent inhibition of PLCPs occurred in vitro when purified SlCYS8 was added to leaf extracts, indicating direct cystatin–PLCP interactions. Activity‐based proteomics revealed that nine different Cathepsin‐L/‐F‐like PLCPs are strongly inhibited by SlCYS8 in leaves. By contrast, the activity of five other Cathepsin‐B/‐H‐like PLCPs, as well as 87 Ser hydrolases, was unaffected by SlCYS8. SlCYS8 expression prevented protein degradation by inhibiting intermediate and mature isoforms of granulin‐containing proteases from the Resistant‐to‐Desiccation‐21 (RD21) PLCP subfamily. Our data underline the key role of endogenous PLCPs on recombinant protein degradation and reveal candidate proteases for depletion strategies. |
| doi_str_mv | 10.1111/pbi.13092 |
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Co‐expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity‐based protein profiling to identify proteases that are inhibited by SlCYS8 in agroinfiltrated Nicotiana benthamiana. We discovered that SlCYS8 selectively suppresses papain‐like cysteine protease (PLCP) activity in both apoplastic fluids and total leaf extracts, while not affecting vacuolar‐processing enzyme and serine hydrolase activity. A robust concentration‐dependent inhibition of PLCPs occurred in vitro when purified SlCYS8 was added to leaf extracts, indicating direct cystatin–PLCP interactions. Activity‐based proteomics revealed that nine different Cathepsin‐L/‐F‐like PLCPs are strongly inhibited by SlCYS8 in leaves. By contrast, the activity of five other Cathepsin‐B/‐H‐like PLCPs, as well as 87 Ser hydrolases, was unaffected by SlCYS8. SlCYS8 expression prevented protein degradation by inhibiting intermediate and mature isoforms of granulin‐containing proteases from the Resistant‐to‐Desiccation‐21 (RD21) PLCP subfamily. Our data underline the key role of endogenous PLCPs on recombinant protein degradation and reveal candidate proteases for depletion strategies.</description><identifier>ISSN: 1467-7644</identifier><identifier>EISSN: 1467-7652</identifier><identifier>DOI: 10.1111/pbi.13092</identifier><identifier>PMID: 30742730</identifier><language>eng</language><publisher>England: John Wiley & Sons, Inc</publisher><subject>activity‐based protein profiling ; Biodegradation ; biotechnology ; Cathepsins ; cystatin ; Cystatins ; Cystatins - pharmacology ; Cysteine ; Cysteine proteinase ; Degradation ; Depletion ; Desiccation ; Grants ; Granulin ; Hydrolase ; Isoforms ; Leaves ; Mass spectrometry ; Nicotiana - enzymology ; Nicotiana benthamiana ; Papain ; papain‐like cysteine proteases ; Peptide Hydrolases - genetics ; Peptides ; Plant extracts ; Plants ; Protease ; protease inhibitor ; Protease inhibitors ; Protease Inhibitors - pharmacology ; protein degradation ; protein synthesis ; Proteinase inhibitors ; Proteins ; Proteolysis ; Proteomics ; Recombinant Proteins ; Scientific imaging ; Serine ; Serine hydrolase ; SlCYS8 ; Tomatoes</subject><ispartof>Plant biotechnology journal, 2019-08, Vol.17 (8), p.1670-1678</ispartof><rights>2019 The Authors. published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.</rights><rights>2019 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.</rights><rights>COPYRIGHT 2019 John Wiley & Sons, Inc.</rights><rights>2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the "License"). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-5177-1142 ; 0000-0003-3310-4773 ; 0000-0002-7093-6838 ; 0000-0002-3692-7487</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fpbi.13092$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fpbi.13092$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,860,1411,11541,27901,27902,45550,45551,46027,46451</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30742730$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jutras, Philippe V.</creatorcontrib><creatorcontrib>Grosse‐Holz, Friederike</creatorcontrib><creatorcontrib>Kaschani, Farnusch</creatorcontrib><creatorcontrib>Kaiser, Markus</creatorcontrib><creatorcontrib>Michaud, Dominique</creatorcontrib><creatorcontrib>Hoorn, Renier A.L.</creatorcontrib><title>Activity‐based proteomics reveals nine target proteases for the recombinant protein‐stabilizing inhibitor SlCYS8 in Nicotiana benthamiana</title><title>Plant biotechnology journal</title><addtitle>Plant Biotechnol J</addtitle><description>Summary
Co‐expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity‐based protein profiling to identify proteases that are inhibited by SlCYS8 in agroinfiltrated Nicotiana benthamiana. We discovered that SlCYS8 selectively suppresses papain‐like cysteine protease (PLCP) activity in both apoplastic fluids and total leaf extracts, while not affecting vacuolar‐processing enzyme and serine hydrolase activity. A robust concentration‐dependent inhibition of PLCPs occurred in vitro when purified SlCYS8 was added to leaf extracts, indicating direct cystatin–PLCP interactions. Activity‐based proteomics revealed that nine different Cathepsin‐L/‐F‐like PLCPs are strongly inhibited by SlCYS8 in leaves. By contrast, the activity of five other Cathepsin‐B/‐H‐like PLCPs, as well as 87 Ser hydrolases, was unaffected by SlCYS8. SlCYS8 expression prevented protein degradation by inhibiting intermediate and mature isoforms of granulin‐containing proteases from the Resistant‐to‐Desiccation‐21 (RD21) PLCP subfamily. Our data underline the key role of endogenous PLCPs on recombinant protein degradation and reveal candidate proteases for depletion strategies.</description><subject>activity‐based protein profiling</subject><subject>Biodegradation</subject><subject>biotechnology</subject><subject>Cathepsins</subject><subject>cystatin</subject><subject>Cystatins</subject><subject>Cystatins - pharmacology</subject><subject>Cysteine</subject><subject>Cysteine proteinase</subject><subject>Degradation</subject><subject>Depletion</subject><subject>Desiccation</subject><subject>Grants</subject><subject>Granulin</subject><subject>Hydrolase</subject><subject>Isoforms</subject><subject>Leaves</subject><subject>Mass spectrometry</subject><subject>Nicotiana - enzymology</subject><subject>Nicotiana benthamiana</subject><subject>Papain</subject><subject>papain‐like cysteine proteases</subject><subject>Peptide Hydrolases - genetics</subject><subject>Peptides</subject><subject>Plant extracts</subject><subject>Plants</subject><subject>Protease</subject><subject>protease inhibitor</subject><subject>Protease inhibitors</subject><subject>Protease Inhibitors - pharmacology</subject><subject>protein degradation</subject><subject>protein synthesis</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Proteomics</subject><subject>Recombinant Proteins</subject><subject>Scientific imaging</subject><subject>Serine</subject><subject>Serine hydrolase</subject><subject>SlCYS8</subject><subject>Tomatoes</subject><issn>1467-7644</issn><issn>1467-7652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNks1u1DAQgCNERX_gwAugSFy47NY_iZ0clxWUShVFKhw4WXYy3p0qcZbYW7Q99QWQeEaehNnuUgTiwMzBo5lvfqyZLHvO2ZSTnK4cTrlktXiUHfFC6YlWpXj8YBfFYXYc4zVjgqtSPckOJdOF0JIdZd9mTcIbTJsfd9-djdDmq3FIMPTYxHyEG7BdzAMGyJMdF5B2YQJj7ocxT0sgqhl6h8GGfRQDFYvJOuzwFsMix7BEh4n4q27--aoiR_4emyGhDTZ3ENLS9lv7aXbgqSE8278n2ae3bz7O300uLs_O57OLyULqWkysdKL1vtDAeC3LRgBzWreldtJ7qZm3zqrWcu-qQuu69aUDb5krFJOMyUqeZK92dWneL2uIyfQYG-g6G2BYRyNKUQjJa_4fKE3AVV1oRejLv9DrYT0G-ogRQpUVq5hgv6mF7cBg8EMabbMtamZakvBaaaKm_6BIW6DVDAE8kv-PhBf75mvXQ2tWI_Z23JhfqybgdAd8pczNQ5wzs70hQzdk7m_IfHh9fm_In8dyuzk</recordid><startdate>201908</startdate><enddate>201908</enddate><creator>Jutras, Philippe V.</creator><creator>Grosse‐Holz, Friederike</creator><creator>Kaschani, Farnusch</creator><creator>Kaiser, Markus</creator><creator>Michaud, Dominique</creator><creator>Hoorn, Renier A.L.</creator><general>John Wiley & Sons, Inc</general><scope>24P</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>L6V</scope><scope>LK8</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-5177-1142</orcidid><orcidid>https://orcid.org/0000-0003-3310-4773</orcidid><orcidid>https://orcid.org/0000-0002-7093-6838</orcidid><orcidid>https://orcid.org/0000-0002-3692-7487</orcidid></search><sort><creationdate>201908</creationdate><title>Activity‐based proteomics reveals nine target proteases for the recombinant protein‐stabilizing inhibitor SlCYS8 in Nicotiana benthamiana</title><author>Jutras, Philippe V. ; Grosse‐Holz, Friederike ; Kaschani, Farnusch ; Kaiser, Markus ; Michaud, Dominique ; Hoorn, Renier A.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g3792-a3b2dff47e01935c2e0b77d57b3ff370faba6da1fb84779df5befa0b460300383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>activity‐based protein profiling</topic><topic>Biodegradation</topic><topic>biotechnology</topic><topic>Cathepsins</topic><topic>cystatin</topic><topic>Cystatins</topic><topic>Cystatins - pharmacology</topic><topic>Cysteine</topic><topic>Cysteine proteinase</topic><topic>Degradation</topic><topic>Depletion</topic><topic>Desiccation</topic><topic>Grants</topic><topic>Granulin</topic><topic>Hydrolase</topic><topic>Isoforms</topic><topic>Leaves</topic><topic>Mass spectrometry</topic><topic>Nicotiana - enzymology</topic><topic>Nicotiana benthamiana</topic><topic>Papain</topic><topic>papain‐like cysteine proteases</topic><topic>Peptide Hydrolases - genetics</topic><topic>Peptides</topic><topic>Plant extracts</topic><topic>Plants</topic><topic>Protease</topic><topic>protease inhibitor</topic><topic>Protease inhibitors</topic><topic>Protease Inhibitors - pharmacology</topic><topic>protein degradation</topic><topic>protein synthesis</topic><topic>Proteinase inhibitors</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Proteomics</topic><topic>Recombinant Proteins</topic><topic>Scientific imaging</topic><topic>Serine</topic><topic>Serine hydrolase</topic><topic>SlCYS8</topic><topic>Tomatoes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jutras, Philippe V.</creatorcontrib><creatorcontrib>Grosse‐Holz, Friederike</creatorcontrib><creatorcontrib>Kaschani, Farnusch</creatorcontrib><creatorcontrib>Kaiser, Markus</creatorcontrib><creatorcontrib>Michaud, Dominique</creatorcontrib><creatorcontrib>Hoorn, Renier A.L.</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Materials Science & Engineering Database (Proquest)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Engineering Collection</collection><collection>Biological Sciences</collection><collection>Biological Science Database</collection><collection>ProQuest Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering collection</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Plant biotechnology journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jutras, Philippe V.</au><au>Grosse‐Holz, Friederike</au><au>Kaschani, Farnusch</au><au>Kaiser, Markus</au><au>Michaud, Dominique</au><au>Hoorn, Renier A.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activity‐based proteomics reveals nine target proteases for the recombinant protein‐stabilizing inhibitor SlCYS8 in Nicotiana benthamiana</atitle><jtitle>Plant biotechnology journal</jtitle><addtitle>Plant Biotechnol J</addtitle><date>2019-08</date><risdate>2019</risdate><volume>17</volume><issue>8</issue><spage>1670</spage><epage>1678</epage><pages>1670-1678</pages><issn>1467-7644</issn><eissn>1467-7652</eissn><abstract>Summary
Co‐expression of protease inhibitors like the tomato cystatin SlCYS8 is useful to increase recombinant protein production in plants, but key proteases involved in protein proteolysis are still unknown. Here, we performed activity‐based protein profiling to identify proteases that are inhibited by SlCYS8 in agroinfiltrated Nicotiana benthamiana. We discovered that SlCYS8 selectively suppresses papain‐like cysteine protease (PLCP) activity in both apoplastic fluids and total leaf extracts, while not affecting vacuolar‐processing enzyme and serine hydrolase activity. A robust concentration‐dependent inhibition of PLCPs occurred in vitro when purified SlCYS8 was added to leaf extracts, indicating direct cystatin–PLCP interactions. Activity‐based proteomics revealed that nine different Cathepsin‐L/‐F‐like PLCPs are strongly inhibited by SlCYS8 in leaves. By contrast, the activity of five other Cathepsin‐B/‐H‐like PLCPs, as well as 87 Ser hydrolases, was unaffected by SlCYS8. SlCYS8 expression prevented protein degradation by inhibiting intermediate and mature isoforms of granulin‐containing proteases from the Resistant‐to‐Desiccation‐21 (RD21) PLCP subfamily. Our data underline the key role of endogenous PLCPs on recombinant protein degradation and reveal candidate proteases for depletion strategies.</abstract><cop>England</cop><pub>John Wiley & Sons, Inc</pub><pmid>30742730</pmid><doi>10.1111/pbi.13092</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-5177-1142</orcidid><orcidid>https://orcid.org/0000-0003-3310-4773</orcidid><orcidid>https://orcid.org/0000-0002-7093-6838</orcidid><orcidid>https://orcid.org/0000-0002-3692-7487</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | activity‐based protein profiling Biodegradation biotechnology Cathepsins cystatin Cystatins Cystatins - pharmacology Cysteine Cysteine proteinase Degradation Depletion Desiccation Grants Granulin Hydrolase Isoforms Leaves Mass spectrometry Nicotiana - enzymology Nicotiana benthamiana Papain papain‐like cysteine proteases Peptide Hydrolases - genetics Peptides Plant extracts Plants Protease protease inhibitor Protease inhibitors Protease Inhibitors - pharmacology protein degradation protein synthesis Proteinase inhibitors Proteins Proteolysis Proteomics Recombinant Proteins Scientific imaging Serine Serine hydrolase SlCYS8 Tomatoes |
| title | Activity‐based proteomics reveals nine target proteases for the recombinant protein‐stabilizing inhibitor SlCYS8 in Nicotiana benthamiana |
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