N-Glycosylation Modification of Plant-Derived Virus-Like Particles : An Application in Vaccines
Plants have been developed as an alternative system to mammalian cells for production of recombinant prophylactic or therapeutic proteins for human and animal use. Effective plant expression systems for recombinant proteins have been established with the optimal combination of gene expression regula...
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| Veröffentlicht in: | BioMed research international 2014-01, Vol.2014 (2014), p.1-8 |
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| creator | Ko, Kisung Lee, Kyung Jin Jeon, Jae-Heung Kim, Hyun-Soon |
| description | Plants have been developed as an alternative system to mammalian cells for production of recombinant prophylactic or therapeutic proteins for human and animal use. Effective plant expression systems for recombinant proteins have been established with the optimal combination of gene expression regulatory elements and control of posttranslational processing of recombinant glycoproteins. In plant, virus-like particles (VLPs), viral “empty shells” which maintain the same structural characteristics of virions but are genome-free, are considered extremely promising as vaccine platforms and therapeutic delivery systems. Unlike microbial fermentation, plants are capable of carrying out N-glycosylation as a posttranslational modification of glycoproteins. Recent advances in the glycoengineering in plant allow human-like glycomodification and optimization of desired glycan structures for enhancing safety and functionality of recombinant pharmaceutical glycoproteins. In this review, the current plant-derived VLP approaches are focused, and N-glycosylation and its in planta modifications are discussed. |
| doi_str_mv | 10.1155/2014/249519 |
| format | Article |
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Effective plant expression systems for recombinant proteins have been established with the optimal combination of gene expression regulatory elements and control of posttranslational processing of recombinant glycoproteins. In plant, virus-like particles (VLPs), viral “empty shells” which maintain the same structural characteristics of virions but are genome-free, are considered extremely promising as vaccine platforms and therapeutic delivery systems. Unlike microbial fermentation, plants are capable of carrying out N-glycosylation as a posttranslational modification of glycoproteins. Recent advances in the glycoengineering in plant allow human-like glycomodification and optimization of desired glycan structures for enhancing safety and functionality of recombinant pharmaceutical glycoproteins. In this review, the current plant-derived VLP approaches are focused, and N-glycosylation and its in planta modifications are discussed.</description><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2014/249519</identifier><identifier>PMID: 24971324</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Puplishing Corporation</publisher><subject>Acids ; Advantages ; Animals ; Antigens ; Bacteria ; Gene Expression ; Glycoproteins - immunology ; Glycosylation ; Health aspects ; Hepatitis ; Humans ; Plants - genetics ; Plants - metabolism ; Plants, Genetically Modified ; Product development ; Prokaryotes ; Protein Processing, Post-Translational ; Proteins ; Review ; Technology, Pharmaceutical - methods ; Tobacco ; Vaccines ; Vaccines, Virus-Like Particle - immunology ; Viral proteins ; Viruses ; Yeast</subject><ispartof>BioMed research international, 2014-01, Vol.2014 (2014), p.1-8</ispartof><rights>Copyright © 2014 Hyun-Soon Kim et al.</rights><rights>COPYRIGHT 2014 John Wiley & Sons, Inc.</rights><rights>Copyright © 2014 Hyun-Soon Kim et al. Hyun-Soon Kim et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2014 Hyun-Soon Kim et al. 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c527t-9fe25a3ceb2315ff0f7445169dec5f388f957f908369c8ac669aba53d53e05c3</citedby><cites>FETCH-LOGICAL-c527t-9fe25a3ceb2315ff0f7445169dec5f388f957f908369c8ac669aba53d53e05c3</cites><orcidid>0000-0002-9054-0689</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4055563/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4055563/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24971324$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Santi, Luca</contributor><creatorcontrib>Ko, Kisung</creatorcontrib><creatorcontrib>Lee, Kyung Jin</creatorcontrib><creatorcontrib>Jeon, Jae-Heung</creatorcontrib><creatorcontrib>Kim, Hyun-Soon</creatorcontrib><title>N-Glycosylation Modification of Plant-Derived Virus-Like Particles : An Application in Vaccines</title><title>BioMed research international</title><addtitle>Biomed Res Int</addtitle><description>Plants have been developed as an alternative system to mammalian cells for production of recombinant prophylactic or therapeutic proteins for human and animal use. Effective plant expression systems for recombinant proteins have been established with the optimal combination of gene expression regulatory elements and control of posttranslational processing of recombinant glycoproteins. In plant, virus-like particles (VLPs), viral “empty shells” which maintain the same structural characteristics of virions but are genome-free, are considered extremely promising as vaccine platforms and therapeutic delivery systems. Unlike microbial fermentation, plants are capable of carrying out N-glycosylation as a posttranslational modification of glycoproteins. Recent advances in the glycoengineering in plant allow human-like glycomodification and optimization of desired glycan structures for enhancing safety and functionality of recombinant pharmaceutical glycoproteins. In this review, the current plant-derived VLP approaches are focused, and N-glycosylation and its in planta modifications are discussed.</description><subject>Acids</subject><subject>Advantages</subject><subject>Animals</subject><subject>Antigens</subject><subject>Bacteria</subject><subject>Gene Expression</subject><subject>Glycoproteins - immunology</subject><subject>Glycosylation</subject><subject>Health aspects</subject><subject>Hepatitis</subject><subject>Humans</subject><subject>Plants - genetics</subject><subject>Plants - metabolism</subject><subject>Plants, Genetically Modified</subject><subject>Product development</subject><subject>Prokaryotes</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Review</subject><subject>Technology, Pharmaceutical - methods</subject><subject>Tobacco</subject><subject>Vaccines</subject><subject>Vaccines, Virus-Like Particle - immunology</subject><subject>Viral proteins</subject><subject>Viruses</subject><subject>Yeast</subject><issn>2314-6133</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkktv1DAQgCMEolXpiTMoEhcECvVrnLgHpFULBWmBHqpeLa8zbl2y9mJnW-2_x6u0y-MCvtiWv_k0M56qek7JO0oBjhih4ogJBVQ9qvYZp6KRVNDHuzPne9VhzjekrI5KouTTaq8EtJQzsV_pr83ZsLExbwYz-hjqL7H3ztvpEl19PpgwNqeY_C329aVP69zM_Xesz00avR0w18f1LNSz1Wp4CPOhvjTW-oD5WfXEmSHj4f1-UF18_HBx8qmZfzv7fDKbNxZYOzbKIQPDLS5K2uAcca0QQKXq0YLjXecUtE6RjktlO2OlVGZhgPfAkYDlB9X7SbtaL5bYWwxjMoNeJb80aaOj8frPl-Cv9VW81YIAgORF8PpekOKPNeZRL322OJTqMa6zpiBlB4q35D9QoB1TlMiCvvoLvYnrFEojCiXatpMF_kVdmQG1Dy6WFO1WqmeCtYQxprautxNlU8w5odtVR4nezoLezoKeZqHQL39vyI59-PkCvJmAax96c-f_YXsxwVgQdGYHC2g5UfwniYPDBA</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Ko, Kisung</creator><creator>Lee, Kyung Jin</creator><creator>Jeon, Jae-Heung</creator><creator>Kim, Hyun-Soon</creator><general>Hindawi Puplishing Corporation</general><general>Hindawi Publishing Corporation</general><general>John Wiley & Sons, Inc</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>3V.</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-9054-0689</orcidid></search><sort><creationdate>20140101</creationdate><title>N-Glycosylation Modification of Plant-Derived Virus-Like Particles : An Application in Vaccines</title><author>Ko, Kisung ; Lee, Kyung Jin ; Jeon, Jae-Heung ; Kim, Hyun-Soon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c527t-9fe25a3ceb2315ff0f7445169dec5f388f957f908369c8ac669aba53d53e05c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acids</topic><topic>Advantages</topic><topic>Animals</topic><topic>Antigens</topic><topic>Bacteria</topic><topic>Gene Expression</topic><topic>Glycoproteins - immunology</topic><topic>Glycosylation</topic><topic>Health aspects</topic><topic>Hepatitis</topic><topic>Humans</topic><topic>Plants - genetics</topic><topic>Plants - metabolism</topic><topic>Plants, Genetically Modified</topic><topic>Product development</topic><topic>Prokaryotes</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Review</topic><topic>Technology, Pharmaceutical - methods</topic><topic>Tobacco</topic><topic>Vaccines</topic><topic>Vaccines, Virus-Like Particle - immunology</topic><topic>Viral proteins</topic><topic>Viruses</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ko, Kisung</creatorcontrib><creatorcontrib>Lee, Kyung Jin</creatorcontrib><creatorcontrib>Jeon, Jae-Heung</creatorcontrib><creatorcontrib>Kim, Hyun-Soon</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BioMed research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ko, Kisung</au><au>Lee, Kyung Jin</au><au>Jeon, Jae-Heung</au><au>Kim, Hyun-Soon</au><au>Santi, Luca</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>N-Glycosylation Modification of Plant-Derived Virus-Like Particles : An Application in Vaccines</atitle><jtitle>BioMed research international</jtitle><addtitle>Biomed Res Int</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>2014</volume><issue>2014</issue><spage>1</spage><epage>8</epage><pages>1-8</pages><issn>2314-6133</issn><eissn>2314-6141</eissn><abstract>Plants have been developed as an alternative system to mammalian cells for production of recombinant prophylactic or therapeutic proteins for human and animal use. Effective plant expression systems for recombinant proteins have been established with the optimal combination of gene expression regulatory elements and control of posttranslational processing of recombinant glycoproteins. In plant, virus-like particles (VLPs), viral “empty shells” which maintain the same structural characteristics of virions but are genome-free, are considered extremely promising as vaccine platforms and therapeutic delivery systems. Unlike microbial fermentation, plants are capable of carrying out N-glycosylation as a posttranslational modification of glycoproteins. Recent advances in the glycoengineering in plant allow human-like glycomodification and optimization of desired glycan structures for enhancing safety and functionality of recombinant pharmaceutical glycoproteins. In this review, the current plant-derived VLP approaches are focused, and N-glycosylation and its in planta modifications are discussed.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Puplishing Corporation</pub><pmid>24971324</pmid><doi>10.1155/2014/249519</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-9054-0689</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Acids Advantages Animals Antigens Bacteria Gene Expression Glycoproteins - immunology Glycosylation Health aspects Hepatitis Humans Plants - genetics Plants - metabolism Plants, Genetically Modified Product development Prokaryotes Protein Processing, Post-Translational Proteins Review Technology, Pharmaceutical - methods Tobacco Vaccines Vaccines, Virus-Like Particle - immunology Viral proteins Viruses Yeast |
| title | N-Glycosylation Modification of Plant-Derived Virus-Like Particles : An Application in Vaccines |
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