Fine‐tuning the N‐glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants
Summary Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing and are able to secrete proteins and perform protein glycosylation. Some biologics have been successfu...
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| Veröffentlicht in: | Plant biotechnology journal 2024-11, Vol.22 (11), p.3018-3027 |
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| creator | Leprovost, S. Plasson, C. Balieu, J. Walet‐Balieu, M‐L. Lerouge, P. Bardor, M. Mathieu‐Rivet, E. |
| description | Summary
Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing and are able to secrete proteins and perform protein glycosylation. Some biologics have been successfully produced in the green microalgae Chlamydomonas reinhardtii. However, post‐translational modifications like glycosylation of these Chlamydomonas‐made biologics have poorly been investigated so far. Therefore, in this study, we report on the first structural investigation of glycans linked to human erythropoietin (hEPO) expressed in a wild‐type C. reinhardtii strain and mutants impaired in key Golgi glycosyltransferases. The glycoproteomic analysis of recombinant hEPO (rhEPO) expressed in the wild‐type strain demonstrated that the three N‐glycosylation sites are 100% glycosylated with mature N‐glycans containing four to five mannose residues and carrying core xylose, core fucose and O‐methyl groups. Moreover, expression in C. reinhardtii insertional mutants defective in xylosyltransferases A and B and fucosyltransferase resulted in drastic decreases of core xylosylation and core fucosylation of glycans N‐linked to the rhEPOs, thus demonstrating that this strategy offers perspectives for humanizing the N‐glycosylation of the Chlamydomonas‐made biologics. |
| doi_str_mv | 10.1111/pbi.14424 |
| format | Article |
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Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing and are able to secrete proteins and perform protein glycosylation. Some biologics have been successfully produced in the green microalgae Chlamydomonas reinhardtii. However, post‐translational modifications like glycosylation of these Chlamydomonas‐made biologics have poorly been investigated so far. Therefore, in this study, we report on the first structural investigation of glycans linked to human erythropoietin (hEPO) expressed in a wild‐type C. reinhardtii strain and mutants impaired in key Golgi glycosyltransferases. The glycoproteomic analysis of recombinant hEPO (rhEPO) expressed in the wild‐type strain demonstrated that the three N‐glycosylation sites are 100% glycosylated with mature N‐glycans containing four to five mannose residues and carrying core xylose, core fucose and O‐methyl groups. Moreover, expression in C. reinhardtii insertional mutants defective in xylosyltransferases A and B and fucosyltransferase resulted in drastic decreases of core xylosylation and core fucosylation of glycans N‐linked to the rhEPOs, thus demonstrating that this strategy offers perspectives for humanizing the N‐glycosylation of the Chlamydomonas‐made biologics.</description><identifier>ISSN: 1467-7644</identifier><identifier>ISSN: 1467-7652</identifier><identifier>EISSN: 1467-7652</identifier><identifier>DOI: 10.1111/pbi.14424</identifier><identifier>PMID: 38968612</identifier><language>eng</language><publisher>England: John Wiley & Sons, Inc</publisher><subject>Algae ; Aquatic microorganisms ; Biological products ; biologics ; Biopharmaceuticals ; Chlamydomonas ; Chlamydomonas reinhardtii ; Chlamydomonas reinhardtii - genetics ; Chlamydomonas reinhardtii - metabolism ; Chromatography ; Complex media ; Erythropoietin ; Erythropoietin - genetics ; Erythropoietin - metabolism ; glycoengineering ; Glycosylation ; Golgi apparatus ; Humans ; Investigations ; Life Sciences ; Mannose ; Microalgae ; Molecular weight ; Mutants ; Mutation - genetics ; Peptides ; Polysaccharides ; Polysaccharides - metabolism ; Proteins ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Strain analysis</subject><ispartof>Plant biotechnology journal, 2024-11, Vol.22 (11), p.3018-3027</ispartof><rights>2024 The Author(s). published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.</rights><rights>2024 The Author(s). Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.</rights><rights>2024. This work is published under http://creativecommons.org/licenses/by-nc/4.0/ (the "License"). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3334-64fd54110d6c26aa3f912290ea782c2c5e71e3bbb3969e2594719cee603d37183</cites><orcidid>0000-0002-3377-6169 ; 0000-0002-0966-903X ; 0000-0002-1031-1916</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.14424$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fpbi.14424$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,864,885,1417,11562,27924,27925,45574,45575,46052,46476</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38968612$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04637398$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Leprovost, S.</creatorcontrib><creatorcontrib>Plasson, C.</creatorcontrib><creatorcontrib>Balieu, J.</creatorcontrib><creatorcontrib>Walet‐Balieu, M‐L.</creatorcontrib><creatorcontrib>Lerouge, P.</creatorcontrib><creatorcontrib>Bardor, M.</creatorcontrib><creatorcontrib>Mathieu‐Rivet, E.</creatorcontrib><title>Fine‐tuning the N‐glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants</title><title>Plant biotechnology journal</title><addtitle>Plant Biotechnol J</addtitle><description>Summary
Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing and are able to secrete proteins and perform protein glycosylation. Some biologics have been successfully produced in the green microalgae Chlamydomonas reinhardtii. However, post‐translational modifications like glycosylation of these Chlamydomonas‐made biologics have poorly been investigated so far. Therefore, in this study, we report on the first structural investigation of glycans linked to human erythropoietin (hEPO) expressed in a wild‐type C. reinhardtii strain and mutants impaired in key Golgi glycosyltransferases. The glycoproteomic analysis of recombinant hEPO (rhEPO) expressed in the wild‐type strain demonstrated that the three N‐glycosylation sites are 100% glycosylated with mature N‐glycans containing four to five mannose residues and carrying core xylose, core fucose and O‐methyl groups. Moreover, expression in C. reinhardtii insertional mutants defective in xylosyltransferases A and B and fucosyltransferase resulted in drastic decreases of core xylosylation and core fucosylation of glycans N‐linked to the rhEPOs, thus demonstrating that this strategy offers perspectives for humanizing the N‐glycosylation of the Chlamydomonas‐made biologics.</description><subject>Algae</subject><subject>Aquatic microorganisms</subject><subject>Biological products</subject><subject>biologics</subject><subject>Biopharmaceuticals</subject><subject>Chlamydomonas</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Chlamydomonas reinhardtii - metabolism</subject><subject>Chromatography</subject><subject>Complex media</subject><subject>Erythropoietin</subject><subject>Erythropoietin - genetics</subject><subject>Erythropoietin - metabolism</subject><subject>glycoengineering</subject><subject>Glycosylation</subject><subject>Golgi apparatus</subject><subject>Humans</subject><subject>Investigations</subject><subject>Life Sciences</subject><subject>Mannose</subject><subject>Microalgae</subject><subject>Molecular weight</subject><subject>Mutants</subject><subject>Mutation - genetics</subject><subject>Peptides</subject><subject>Polysaccharides</subject><subject>Polysaccharides - metabolism</subject><subject>Proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Strain analysis</subject><issn>1467-7644</issn><issn>1467-7652</issn><issn>1467-7652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kc1u1DAUhSNERUthwQugSGxgMa3_Yscr1I4orTQCFrC2HOdm4iqxB9spyo5H4Bl5EjyddgqV8Ma-9nfOtX2K4hVGJziP001jTzBjhD0pjjDjYiF4RZ7u14wdFs9jvEaIYF7xZ8UhrSWvOSZHhb-wDn7__JUmZ926TD2Un3K5Hmbj4zzoZL0rfVcGMH5srNMulf00aldCmFMf_MZbSNaVU9zql_2gx7n1o3c6ZpF1vQ5tsrYcp5S18UVx0Okhwsu7-bj4dvHh6_Jysfr88Wp5tloYSilbcNa1FcMYtdwQrjXtJCZEItCiJoaYCgQG2jQNlVwCqSQTWBoAjmhLBa7pcfF-57uZmhFaAy4FPahNsKMOs_Laqn9PnO3V2t8ojCuEZI2yw7udQ_9Id3m2Uts9xDgVVNY3OLNv77oF_32CmNRoo4Fh0A78FBVFgpNacCEz-uYReu2n4PJfKIqxRBzlmB6am-BjDNDtb4CR2maucubqNvPMvv77qXvyPuQMnO6AH3aA-f9O6sv51c7yDyD_uS8</recordid><startdate>202411</startdate><enddate>202411</enddate><creator>Leprovost, S.</creator><creator>Plasson, C.</creator><creator>Balieu, J.</creator><creator>Walet‐Balieu, M‐L.</creator><creator>Lerouge, P.</creator><creator>Bardor, M.</creator><creator>Mathieu‐Rivet, E.</creator><general>John Wiley & Sons, Inc</general><general>Wiley</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>COVID</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>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-3377-6169</orcidid><orcidid>https://orcid.org/0000-0002-0966-903X</orcidid><orcidid>https://orcid.org/0000-0002-1031-1916</orcidid></search><sort><creationdate>202411</creationdate><title>Fine‐tuning the N‐glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants</title><author>Leprovost, S. ; 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Microalgae are considered as attractive expression systems for the production of biologics. As photosynthetic unicellular organisms, they do not require costly and complex media for growing and are able to secrete proteins and perform protein glycosylation. Some biologics have been successfully produced in the green microalgae Chlamydomonas reinhardtii. However, post‐translational modifications like glycosylation of these Chlamydomonas‐made biologics have poorly been investigated so far. Therefore, in this study, we report on the first structural investigation of glycans linked to human erythropoietin (hEPO) expressed in a wild‐type C. reinhardtii strain and mutants impaired in key Golgi glycosyltransferases. The glycoproteomic analysis of recombinant hEPO (rhEPO) expressed in the wild‐type strain demonstrated that the three N‐glycosylation sites are 100% glycosylated with mature N‐glycans containing four to five mannose residues and carrying core xylose, core fucose and O‐methyl groups. Moreover, expression in C. reinhardtii insertional mutants defective in xylosyltransferases A and B and fucosyltransferase resulted in drastic decreases of core xylosylation and core fucosylation of glycans N‐linked to the rhEPOs, thus demonstrating that this strategy offers perspectives for humanizing the N‐glycosylation of the Chlamydomonas‐made biologics.</abstract><cop>England</cop><pub>John Wiley & Sons, Inc</pub><pmid>38968612</pmid><doi>10.1111/pbi.14424</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-3377-6169</orcidid><orcidid>https://orcid.org/0000-0002-0966-903X</orcidid><orcidid>https://orcid.org/0000-0002-1031-1916</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Algae Aquatic microorganisms Biological products biologics Biopharmaceuticals Chlamydomonas Chlamydomonas reinhardtii Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism Chromatography Complex media Erythropoietin Erythropoietin - genetics Erythropoietin - metabolism glycoengineering Glycosylation Golgi apparatus Humans Investigations Life Sciences Mannose Microalgae Molecular weight Mutants Mutation - genetics Peptides Polysaccharides Polysaccharides - metabolism Proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Strain analysis |
| title | Fine‐tuning the N‐glycosylation of recombinant human erythropoietin using Chlamydomonas reinhardtii mutants |
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