Expression optimization, purification and in vitro characterization of human epidermal growth factor produced in Nicotiana benthamiana.
Identifieur interne : 000043 ( Main/Exploration ); précédent : 000042; suivant : 000044Expression optimization, purification and in vitro characterization of human epidermal growth factor produced in Nicotiana benthamiana.
Auteurs : Oranicha Hanittinan [Thaïlande] ; Yamin Oo [Thaïlande] ; Chatchai Chaotham [Thaïlande] ; Kaewta Rattanapisit [Thaïlande] ; Balamurugan Shanmugaraj [Thaïlande] ; Waranyoo Phoolcharoen [Thaïlande]Source :
- Biotechnology reports (Amsterdam, Netherlands) [ 2215-017X ] ; 2020.
Abstract
Human epidermal growth factor (hEGF) has gained clinical importance due to its ability to promote wound healing. Due to its commercial applications and high market demand, recombinant EGF has been produced in several forms. Currently, plant expression system is considered as potential alternative for low-cost recombinant protein production. Hence, this study focused on improving the production of hEGF in plants by effective gene construct design and optimizing the Agrobacterium culture conditions for high protein production. In this context, hEGF gene was cloned into plant geminiviral expression vector pBYR2e and transformed in to N. benthamiana leaves via., agroinfiltration. The recombinant hEGF was purified from the plant crude extracts by single-step affinity chromatography. Furthermore, the plant-produced hEGF has shown to promote cell migration comparable to commercial hEGF in HaCaT cells in vitro. These results indicated the potential of plant expression system for the production of recombinant hEGF for tissue engineering applications.
DOI: 10.1016/j.btre.2020.e00524
PubMed: 32953470
PubMed Central: PMC7486445
Affiliations:
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Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok</wicri:regionArea><wicri:noRegion>Bangkok</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok</wicri:regionArea><wicri:noRegion>Bangkok</wicri:noRegion></affiliation></author><author><name sortKey="Shanmugaraj, Balamurugan" sort="Shanmugaraj, Balamurugan" uniqKey="Shanmugaraj B" first="Balamurugan" last="Shanmugaraj">Balamurugan Shanmugaraj</name><affiliation wicri:level="1"><nlm:affiliation>Department of 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wicri:level="1"><nlm:affiliation>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok</wicri:regionArea><wicri:noRegion>Bangkok</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok, Thailand.</nlm:affiliation><country xml:lang="fr">Thaïlande</country><wicri:regionArea>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok</wicri:regionArea><wicri:noRegion>Bangkok</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biotechnology reports (Amsterdam, Netherlands)</title><idno type="ISSN">2215-017X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human epidermal growth factor (hEGF) has gained clinical importance due to its ability to promote wound healing. Due to its commercial applications and high market demand, recombinant EGF has been produced in several forms. Currently, plant expression system is considered as potential alternative for low-cost recombinant protein production. Hence, this study focused on improving the production of hEGF in plants by effective gene construct design and optimizing the <i>Agrobacterium</i> culture conditions for high protein production. In this context, hEGF gene was cloned into plant geminiviral expression vector pBYR2e and transformed in to <i>N. benthamiana</i> leaves <i>via</i>., agroinfiltration. The recombinant hEGF was purified from the plant crude extracts by single-step affinity chromatography. Furthermore, the plant-produced hEGF has shown to promote cell migration comparable to commercial hEGF in HaCaT cells <i>in vitro</i>. These results indicated the potential of plant expression system for the production of recombinant hEGF for tissue engineering applications.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32953470</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2215-017X</ISSN><JournalIssue CitedMedium="Print"><Volume>28</Volume><PubDate><Year>2020</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biotechnology reports (Amsterdam, Netherlands)</Title><ISOAbbreviation>Biotechnol Rep (Amst)</ISOAbbreviation></Journal><ArticleTitle>Expression optimization, purification and <i>in vitro</i> characterization of human epidermal growth factor produced in <i>Nicotiana benthamiana</i>.</ArticleTitle><Pagination><MedlinePgn>e00524</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.btre.2020.e00524</ELocationID><Abstract><AbstractText>Human epidermal growth factor (hEGF) has gained clinical importance due to its ability to promote wound healing. Due to its commercial applications and high market demand, recombinant EGF has been produced in several forms. Currently, plant expression system is considered as potential alternative for low-cost recombinant protein production. Hence, this study focused on improving the production of hEGF in plants by effective gene construct design and optimizing the <i>Agrobacterium</i> culture conditions for high protein production. In this context, hEGF gene was cloned into plant geminiviral expression vector pBYR2e and transformed in to <i>N. benthamiana</i> leaves <i>via</i>., agroinfiltration. The recombinant hEGF was purified from the plant crude extracts by single-step affinity chromatography. Furthermore, the plant-produced hEGF has shown to promote cell migration comparable to commercial hEGF in HaCaT cells <i>in vitro</i>. These results indicated the potential of plant expression system for the production of recombinant hEGF for tissue engineering applications.</AbstractText><CopyrightInformation>© 2020 The Authors.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hanittinan</LastName><ForeName>Oranicha</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oo</LastName><ForeName>Yamin</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaotham</LastName><ForeName>Chatchai</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Cell-based Drug and Health Products Development Research Unit, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rattanapisit</LastName><ForeName>Kaewta</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shanmugaraj</LastName><ForeName>Balamurugan</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Phoolcharoen</LastName><ForeName>Waranyoo</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Pharmacognosy and Pharmaceutical Botany, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Research Unit for Plant-produced Pharmaceuticals, Chulalongkorn University, Bangkok, Thailand.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biotechnol Rep (Amst)</MedlineTA><NlmUniqueID>101637426</NlmUniqueID><ISSNLinking>2215-017X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Human epidermal growth factor</Keyword><Keyword MajorTopicYN="N">Nicotiana benthamiana</Keyword><Keyword MajorTopicYN="N">Plant-produced protein</Keyword><Keyword MajorTopicYN="N">Recombinant protein</Keyword><Keyword MajorTopicYN="N">Transient expression</Keyword></KeywordList><CoiStatement>The authors declare no conflicts of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>07</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>08</Month><Day>13</Day></PubMedPubDate><PubMedPubDate 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name="Thaïlande"><noRegion><name sortKey="Hanittinan, Oranicha" sort="Hanittinan, Oranicha" uniqKey="Hanittinan O" first="Oranicha" last="Hanittinan">Oranicha Hanittinan</name></noRegion><name sortKey="Chaotham, Chatchai" sort="Chaotham, Chatchai" uniqKey="Chaotham C" first="Chatchai" last="Chaotham">Chatchai Chaotham</name><name sortKey="Chaotham, Chatchai" sort="Chaotham, Chatchai" uniqKey="Chaotham C" first="Chatchai" last="Chaotham">Chatchai Chaotham</name><name sortKey="Oo, Yamin" sort="Oo, Yamin" uniqKey="Oo Y" first="Yamin" last="Oo">Yamin Oo</name><name sortKey="Phoolcharoen, Waranyoo" sort="Phoolcharoen, Waranyoo" uniqKey="Phoolcharoen W" first="Waranyoo" last="Phoolcharoen">Waranyoo Phoolcharoen</name><name sortKey="Phoolcharoen, Waranyoo" sort="Phoolcharoen, Waranyoo" uniqKey="Phoolcharoen W" first="Waranyoo" last="Phoolcharoen">Waranyoo Phoolcharoen</name><name sortKey="Rattanapisit, Kaewta" sort="Rattanapisit, Kaewta" uniqKey="Rattanapisit K" first="Kaewta" last="Rattanapisit">Kaewta Rattanapisit</name><name sortKey="Rattanapisit, Kaewta" sort="Rattanapisit, Kaewta" uniqKey="Rattanapisit K" first="Kaewta" last="Rattanapisit">Kaewta Rattanapisit</name><name sortKey="Shanmugaraj, Balamurugan" sort="Shanmugaraj, Balamurugan" uniqKey="Shanmugaraj B" first="Balamurugan" last="Shanmugaraj">Balamurugan Shanmugaraj</name><name sortKey="Shanmugaraj, Balamurugan" sort="Shanmugaraj, Balamurugan" uniqKey="Shanmugaraj B" first="Balamurugan" last="Shanmugaraj">Balamurugan Shanmugaraj</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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