Expression of single-domain antibody in different systems
Camelid single-domain antibodies (sdAbs, VHHs, or Nanobodies®) are types of antibody fragments that are composed of the heavy-chain variable domain only. These VHHs possess unique structural and functional features, as they are small in size and exhibit thermal stability and high solubility. Compare...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2018, Vol.102 (2), p.539-551 |
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| creator | Liu, Yongkang Huang, He |
| description | Camelid single-domain antibodies (sdAbs, VHHs, or Nanobodies®) are types of antibody fragments that are composed of the heavy-chain variable domain only. These VHHs possess unique structural and functional features, as they are small in size and exhibit thermal stability and high solubility. Compared to conventional antibodies, VHHs can be manufactured in microorganisms to significantly save on cost, labor, and time since VHHs lack the Fc domain with its N-linked oligosaccharide. Until now, VHHs have been expressed in several kinds of production systems, ranging from prokaryotic cells, yeasts, fungi, insect cells, and mammalian cell lines, to plants. In this review, we focus on the recent production of VHHs, introduce different platforms, and summarize the current state of this area and its future trends. Finally, the first potential VHH product, produced in
Pichia pastoris
, will probably be available on the market in 2018; thus, it is of great importance to give this antibody fragment timely attention. This is the first review concerning the production of VHHs in laboratory settings. |
| doi_str_mv | 10.1007/s00253-017-8644-3 |
| format | Article |
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Pichia pastoris
, will probably be available on the market in 2018; thus, it is of great importance to give this antibody fragment timely attention. This is the first review concerning the production of VHHs in laboratory settings.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-017-8644-3</identifier><identifier>PMID: 29177623</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Animals ; Antibodies ; Biomedical and Life Sciences ; Biotechnology ; Capital costs ; Cell Line ; Cell lines ; Chemical bonds ; Cytoplasm ; E coli ; Escherichia coli - metabolism ; Fungi ; Fungi - metabolism ; Genetic Engineering ; Immunoglobulin Heavy Chains - biosynthesis ; Insect cells ; Laboratories ; Life Sciences ; Medical research ; Microbial Genetics and Genomics ; Microbiology ; Microorganisms ; Mini-Review ; Nanobodies ; Physiological aspects ; Pichia - metabolism ; Pichia pastoris ; Plants - metabolism ; Production processes ; Proteins ; R&D ; Research & development ; Saccharomyces ; Single-Domain Antibodies - biosynthesis ; Structure-function relationships ; Thermal stability ; Yeast ; Yeasts</subject><ispartof>Applied microbiology and biotechnology, 2018, Vol.102 (2), p.539-551</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2017</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2017). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-cae6d385d6fa8cc71295fe10e8e7c5c8afac97b9ccbfc28f56a6d25a643eb4b23</citedby><cites>FETCH-LOGICAL-c510t-cae6d385d6fa8cc71295fe10e8e7c5c8afac97b9ccbfc28f56a6d25a643eb4b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-017-8644-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-017-8644-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29177623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Yongkang</creatorcontrib><creatorcontrib>Huang, He</creatorcontrib><title>Expression of single-domain antibody in different systems</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Camelid single-domain antibodies (sdAbs, VHHs, or Nanobodies®) are types of antibody fragments that are composed of the heavy-chain variable domain only. These VHHs possess unique structural and functional features, as they are small in size and exhibit thermal stability and high solubility. Compared to conventional antibodies, VHHs can be manufactured in microorganisms to significantly save on cost, labor, and time since VHHs lack the Fc domain with its N-linked oligosaccharide. Until now, VHHs have been expressed in several kinds of production systems, ranging from prokaryotic cells, yeasts, fungi, insect cells, and mammalian cell lines, to plants. In this review, we focus on the recent production of VHHs, introduce different platforms, and summarize the current state of this area and its future trends. Finally, the first potential VHH product, produced in
Pichia pastoris
, will probably be available on the market in 2018; thus, it is of great importance to give this antibody fragment timely attention. This is the first review concerning the production of VHHs in laboratory settings.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Capital costs</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Chemical bonds</subject><subject>Cytoplasm</subject><subject>E coli</subject><subject>Escherichia coli - metabolism</subject><subject>Fungi</subject><subject>Fungi - metabolism</subject><subject>Genetic Engineering</subject><subject>Immunoglobulin Heavy Chains - biosynthesis</subject><subject>Insect cells</subject><subject>Laboratories</subject><subject>Life Sciences</subject><subject>Medical research</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Mini-Review</subject><subject>Nanobodies</subject><subject>Physiological aspects</subject><subject>Pichia - metabolism</subject><subject>Pichia pastoris</subject><subject>Plants - metabolism</subject><subject>Production processes</subject><subject>Proteins</subject><subject>R&D</subject><subject>Research & development</subject><subject>Saccharomyces</subject><subject>Single-Domain Antibodies - biosynthesis</subject><subject>Structure-function relationships</subject><subject>Thermal stability</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><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>eNp1kdtrFDEYxYModrv6B_giA77Yh6m5TG6PpVQtFAQvzyGT-bKkzCRrMgPd_94MWy8rSh4S8v3OSQ4HoVcEXxKM5buCMeWsxUS2SnRdy56gDekYbbEg3VO0qQPeSq7VGTov5R5jQpUQz9EZ1URKQdkG6ZuHfYZSQopN8k0JcTdCO6TJhtjYOIc-DYemnofgPWSIc1MOZYapvEDPvB0LvHzct-jb-5uv1x_bu08fbq-v7lrHCZ5bZ0EMTPFBeKuck4Rq7oFgUCAdd8p667TstXO9d1R5LqwYKLeiY9B3PWVb9Pbou8_p-wJlNlMoDsbRRkhLMUQLrRmnNfgWvfkLvU9LjvV3KyW15gzL39TOjmBC9GnO1q2m5qraSKU5XZ-9_AdV1wBTcCmCD_X-RHBxIqjMDA_zzi6lmNsvn09ZcmRdTqVk8Gafw2TzwRBs1mrNsVpTGzRrtYZVzevHcEs_wfBL8bPLCtAjUOoo7iD_kf6_rj8AOqasCw</recordid><startdate>2018</startdate><enddate>2018</enddate><creator>Liu, Yongkang</creator><creator>Huang, He</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>2018</creationdate><title>Expression of single-domain antibody in different systems</title><author>Liu, Yongkang ; Huang, He</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-cae6d385d6fa8cc71295fe10e8e7c5c8afac97b9ccbfc28f56a6d25a643eb4b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Capital costs</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Chemical bonds</topic><topic>Cytoplasm</topic><topic>E coli</topic><topic>Escherichia coli - 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Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Yongkang</au><au>Huang, He</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of single-domain antibody in different systems</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2018</date><risdate>2018</risdate><volume>102</volume><issue>2</issue><spage>539</spage><epage>551</epage><pages>539-551</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Camelid single-domain antibodies (sdAbs, VHHs, or Nanobodies®) are types of antibody fragments that are composed of the heavy-chain variable domain only. These VHHs possess unique structural and functional features, as they are small in size and exhibit thermal stability and high solubility. Compared to conventional antibodies, VHHs can be manufactured in microorganisms to significantly save on cost, labor, and time since VHHs lack the Fc domain with its N-linked oligosaccharide. Until now, VHHs have been expressed in several kinds of production systems, ranging from prokaryotic cells, yeasts, fungi, insect cells, and mammalian cell lines, to plants. In this review, we focus on the recent production of VHHs, introduce different platforms, and summarize the current state of this area and its future trends. Finally, the first potential VHH product, produced in
Pichia pastoris
, will probably be available on the market in 2018; thus, it is of great importance to give this antibody fragment timely attention. This is the first review concerning the production of VHHs in laboratory settings.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29177623</pmid><doi>10.1007/s00253-017-8644-3</doi><tpages>13</tpages></addata></record> |
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| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2018, Vol.102 (2), p.539-551 |
| issn | 0175-7598 1432-0614 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Animals Antibodies Biomedical and Life Sciences Biotechnology Capital costs Cell Line Cell lines Chemical bonds Cytoplasm E coli Escherichia coli - metabolism Fungi Fungi - metabolism Genetic Engineering Immunoglobulin Heavy Chains - biosynthesis Insect cells Laboratories Life Sciences Medical research Microbial Genetics and Genomics Microbiology Microorganisms Mini-Review Nanobodies Physiological aspects Pichia - metabolism Pichia pastoris Plants - metabolism Production processes Proteins R&D Research & development Saccharomyces Single-Domain Antibodies - biosynthesis Structure-function relationships Thermal stability Yeast Yeasts |
| title | Expression of single-domain antibody in different systems |
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