Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris
Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expre...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2023-07, Vol.107 (14), p.4543-4551 |
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| creator | Lu, Zequn Liu, Ning Huang, Huoqing Wang, Yuan Tu, Tao Qin, Xing Wang, Xiaolu Zhang, Jie Su, Xiaoyun Tian, Jian Bai, Yingguo Luo, Huiying Yao, Bin Zhang, Honglian |
| description | Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expression levels in various expression systems and hard to meet the needs of clinical and scientific research. Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the
Pichia pastoris
(
P. pastoris
) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in
P. pastoris
, which could be used for both clinical and scientific applications.
Key points
•
Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system.
•
Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1.
•
High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor. |
| doi_str_mv | 10.1007/s00253-023-12606-0 |
| format | Article |
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Pichia pastoris
(
P. pastoris
) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in
P. pastoris
, which could be used for both clinical and scientific applications.
Key points
•
Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system.
•
Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1.
•
High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-023-12606-0</identifier><identifier>PMID: 37261455</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Analysis ; Biological activity ; Biomedical and Life Sciences ; Bioreactors ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Cell proliferation ; Fermentation ; Gene expression ; Genetic aspects ; Growth factors ; Identification and classification ; Insulin-like growth factor 1 ; Insulin-like growth factor I ; Insulin-like growth factors ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Pichia pastoris ; Proteins ; Therapeutic targets ; Xylanase ; Xylanases ; Yeast ; Yeast fungi</subject><ispartof>Applied microbiology and biotechnology, 2023-07, Vol.107 (14), p.4543-4551</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><rights>COPYRIGHT 2023 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-e823c7cec7dec7cf23a0cab226dd0e6174054863f160eb47305ad193e2d376013</citedby><cites>FETCH-LOGICAL-c442t-e823c7cec7dec7cf23a0cab226dd0e6174054863f160eb47305ad193e2d376013</cites><orcidid>0000-0002-6822-5359</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-023-12606-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-023-12606-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27907,27908,41471,42540,51302</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37261455$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lu, Zequn</creatorcontrib><creatorcontrib>Liu, Ning</creatorcontrib><creatorcontrib>Huang, Huoqing</creatorcontrib><creatorcontrib>Wang, Yuan</creatorcontrib><creatorcontrib>Tu, Tao</creatorcontrib><creatorcontrib>Qin, Xing</creatorcontrib><creatorcontrib>Wang, Xiaolu</creatorcontrib><creatorcontrib>Zhang, Jie</creatorcontrib><creatorcontrib>Su, Xiaoyun</creatorcontrib><creatorcontrib>Tian, Jian</creatorcontrib><creatorcontrib>Bai, Yingguo</creatorcontrib><creatorcontrib>Luo, Huiying</creatorcontrib><creatorcontrib>Yao, Bin</creatorcontrib><creatorcontrib>Zhang, Honglian</creatorcontrib><title>Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expression levels in various expression systems and hard to meet the needs of clinical and scientific research. Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the
Pichia pastoris
(
P. pastoris
) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in
P. pastoris
, which could be used for both clinical and scientific applications.
Key points
•
Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system.
•
Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1.
•
High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.</description><subject>Analysis</subject><subject>Biological activity</subject><subject>Biomedical and Life Sciences</subject><subject>Bioreactors</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Cell proliferation</subject><subject>Fermentation</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>Growth factors</subject><subject>Identification and classification</subject><subject>Insulin-like growth factor 1</subject><subject>Insulin-like growth factor I</subject><subject>Insulin-like growth factors</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Pichia pastoris</subject><subject>Proteins</subject><subject>Therapeutic targets</subject><subject>Xylanase</subject><subject>Xylanases</subject><subject>Yeast</subject><subject>Yeast 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expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris</title><author>Lu, Zequn ; Liu, Ning ; Huang, Huoqing ; Wang, Yuan ; Tu, Tao ; Qin, Xing ; Wang, Xiaolu ; Zhang, Jie ; Su, Xiaoyun ; Tian, Jian ; Bai, Yingguo ; Luo, Huiying ; Yao, Bin ; Zhang, Honglian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-e823c7cec7dec7cf23a0cab226dd0e6174054863f160eb47305ad193e2d376013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Analysis</topic><topic>Biological activity</topic><topic>Biomedical and Life Sciences</topic><topic>Bioreactors</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Cell proliferation</topic><topic>Fermentation</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>Growth factors</topic><topic>Identification and classification</topic><topic>Insulin-like growth factor 1</topic><topic>Insulin-like growth factor I</topic><topic>Insulin-like growth factors</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Pichia pastoris</topic><topic>Proteins</topic><topic>Therapeutic targets</topic><topic>Xylanase</topic><topic>Xylanases</topic><topic>Yeast</topic><topic>Yeast fungi</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Zequn</creatorcontrib><creatorcontrib>Liu, Ning</creatorcontrib><creatorcontrib>Huang, Huoqing</creatorcontrib><creatorcontrib>Wang, Yuan</creatorcontrib><creatorcontrib>Tu, Tao</creatorcontrib><creatorcontrib>Qin, Xing</creatorcontrib><creatorcontrib>Wang, Xiaolu</creatorcontrib><creatorcontrib>Zhang, Jie</creatorcontrib><creatorcontrib>Su, Xiaoyun</creatorcontrib><creatorcontrib>Tian, Jian</creatorcontrib><creatorcontrib>Bai, Yingguo</creatorcontrib><creatorcontrib>Luo, Huiying</creatorcontrib><creatorcontrib>Yao, 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pastoris</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2023-07-01</date><risdate>2023</risdate><volume>107</volume><issue>14</issue><spage>4543</spage><epage>4551</epage><pages>4543-4551</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expression levels in various expression systems and hard to meet the needs of clinical and scientific research. Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the
Pichia pastoris
(
P. pastoris
) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in
P. pastoris
, which could be used for both clinical and scientific applications.
Key points
•
Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system.
•
Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1.
•
High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>37261455</pmid><doi>10.1007/s00253-023-12606-0</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-6822-5359</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2023-07, Vol.107 (14), p.4543-4551 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2821639691 |
| source | SpringerLink Journals - AutoHoldings |
| subjects | Analysis Biological activity Biomedical and Life Sciences Bioreactors Biotechnologically Relevant Enzymes and Proteins Biotechnology Cell proliferation Fermentation Gene expression Genetic aspects Growth factors Identification and classification Insulin-like growth factor 1 Insulin-like growth factor I Insulin-like growth factors Life Sciences Microbial Genetics and Genomics Microbiology Pichia pastoris Proteins Therapeutic targets Xylanase Xylanases Yeast Yeast fungi |
| title | Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris |
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