Expression, Purification, and Characterization of Hepatitis B Virus Surface Antigens (HBsAg) in Yeast Pichia Pastoris
Prevention of the prevalence of HB depends upon the development of efficient diagnostic reagent and preventive vaccine. Pichia pastoris offers many advantages over the other expression systems in the production of recombinant HBsAg. In this study, we reported that the recombinant P. pastoris strains...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2009-08, Vol.158 (2), p.432-444 |
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| creator | Liu, Rushi Lin, Qinlu Sun, Yi Lu, Xiangyang Qiu, Yilan Li, Ye Guo, Xiangrong |
| description | Prevention of the prevalence of HB depends upon the development of efficient diagnostic reagent and preventive vaccine. Pichia pastoris offers many advantages over the other expression systems in the production of recombinant HBsAg. In this study, we reported that the recombinant P. pastoris strains were cultured in shake flasks and then scaled up in a 5.0-l bioreactor: approximately 27 mg/l of the protein and the maximal cell OD at 600 nm of 310 were achieved in the bioreactor. The recombinant HBsAg was purified by three steps of purification procedures. SDS-PAGE showed that the purified recombinant HBsAg constituted only one homogeneous band of ~24 kDa. CsCl density gradient ultracentrifugation assay indicated that the density of the HBsAg was 1.2 mg/ml, which was in agreement with the natural HBsAg, the HBsAg expressed in Saccharomyces cerevisiae and in mammalian cells. Electron microscope observation revealed that the purified recombinant HBsAg was homogeneous 22-nm particles, suggesting the HBsAg expressed in P. pastoris was self-assembled to virus-like structures. Competitive ELISA indicated that P. pastoris-derived HBsAg possessed the excellent immunoreaction with anti-HBsAg. Animal immunization showed that the immunogenicity of P. pastoris-derived HBsAg was superior to that of S. cerevisiae-derived HBsAg. Together, our results demonstrated that the recombinant HBsAg expressed in P. pastoris could provide promising, inexpensive, and large-scale materials for the diagnostic reagent and vaccine to prevent HBV infection. |
| doi_str_mv | 10.1007/s12010-009-8527-x |
| format | Article |
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Pichia pastoris offers many advantages over the other expression systems in the production of recombinant HBsAg. In this study, we reported that the recombinant P. pastoris strains were cultured in shake flasks and then scaled up in a 5.0-l bioreactor: approximately 27 mg/l of the protein and the maximal cell OD at 600 nm of 310 were achieved in the bioreactor. The recombinant HBsAg was purified by three steps of purification procedures. SDS-PAGE showed that the purified recombinant HBsAg constituted only one homogeneous band of ~24 kDa. CsCl density gradient ultracentrifugation assay indicated that the density of the HBsAg was 1.2 mg/ml, which was in agreement with the natural HBsAg, the HBsAg expressed in Saccharomyces cerevisiae and in mammalian cells. Electron microscope observation revealed that the purified recombinant HBsAg was homogeneous 22-nm particles, suggesting the HBsAg expressed in P. pastoris was self-assembled to virus-like structures. Competitive ELISA indicated that P. pastoris-derived HBsAg possessed the excellent immunoreaction with anti-HBsAg. Animal immunization showed that the immunogenicity of P. pastoris-derived HBsAg was superior to that of S. cerevisiae-derived HBsAg. Together, our results demonstrated that the recombinant HBsAg expressed in P. pastoris could provide promising, inexpensive, and large-scale materials for the diagnostic reagent and vaccine to prevent HBV infection.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-009-8527-x</identifier><identifier>PMID: 19184543</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: New York : Humana Press Inc</publisher><subject>Animals ; Biochemistry ; Biological and medical sciences ; Bioreactors ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Fungal ; Hepatitis ; Hepatitis B Surface Antigens - biosynthesis ; Hepatitis B Surface Antigens - genetics ; Hepatitis B Surface Antigens - immunology ; Hepatitis B Surface Antigens - isolation & purification ; Hepatitis B virus ; Immunization ; Immunogenicity ; Mice ; Mice, Inbred BALB C ; Pichia - genetics ; Pichia - metabolism ; Pichia pastoris ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Recombinant Proteins - isolation & purification ; Saccharomyces cerevisiae ; Ultracentrifugation ; Vaccines ; Yeast ; Yeasts</subject><ispartof>Applied biochemistry and biotechnology, 2009-08, Vol.158 (2), p.432-444</ispartof><rights>Humana Press 2009</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-b115db5ec51a5c7f5964b7c07bb0186f8400e803b2539970fd190c38a5d954673</citedby><cites>FETCH-LOGICAL-c454t-b115db5ec51a5c7f5964b7c07bb0186f8400e803b2539970fd190c38a5d954673</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/s12010-009-8527-x$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-009-8527-x$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21752567$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19184543$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Rushi</creatorcontrib><creatorcontrib>Lin, Qinlu</creatorcontrib><creatorcontrib>Sun, Yi</creatorcontrib><creatorcontrib>Lu, Xiangyang</creatorcontrib><creatorcontrib>Qiu, Yilan</creatorcontrib><creatorcontrib>Li, Ye</creatorcontrib><creatorcontrib>Guo, Xiangrong</creatorcontrib><title>Expression, Purification, and Characterization of Hepatitis B Virus Surface Antigens (HBsAg) in Yeast Pichia Pastoris</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Prevention of the prevalence of HB depends upon the development of efficient diagnostic reagent and preventive vaccine. Pichia pastoris offers many advantages over the other expression systems in the production of recombinant HBsAg. In this study, we reported that the recombinant P. pastoris strains were cultured in shake flasks and then scaled up in a 5.0-l bioreactor: approximately 27 mg/l of the protein and the maximal cell OD at 600 nm of 310 were achieved in the bioreactor. The recombinant HBsAg was purified by three steps of purification procedures. SDS-PAGE showed that the purified recombinant HBsAg constituted only one homogeneous band of ~24 kDa. CsCl density gradient ultracentrifugation assay indicated that the density of the HBsAg was 1.2 mg/ml, which was in agreement with the natural HBsAg, the HBsAg expressed in Saccharomyces cerevisiae and in mammalian cells. Electron microscope observation revealed that the purified recombinant HBsAg was homogeneous 22-nm particles, suggesting the HBsAg expressed in P. pastoris was self-assembled to virus-like structures. Competitive ELISA indicated that P. pastoris-derived HBsAg possessed the excellent immunoreaction with anti-HBsAg. Animal immunization showed that the immunogenicity of P. pastoris-derived HBsAg was superior to that of S. cerevisiae-derived HBsAg. Together, our results demonstrated that the recombinant HBsAg expressed in P. pastoris could provide promising, inexpensive, and large-scale materials for the diagnostic reagent and vaccine to prevent HBV infection.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Bioreactors</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Hepatitis</subject><subject>Hepatitis B Surface Antigens - biosynthesis</subject><subject>Hepatitis B Surface Antigens - genetics</subject><subject>Hepatitis B Surface Antigens - immunology</subject><subject>Hepatitis B Surface Antigens - isolation & purification</subject><subject>Hepatitis B virus</subject><subject>Immunization</subject><subject>Immunogenicity</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Pichia - genetics</subject><subject>Pichia - metabolism</subject><subject>Pichia pastoris</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Saccharomyces cerevisiae</subject><subject>Ultracentrifugation</subject><subject>Vaccines</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkVGLEzEUhYMobl39Ab5oEBQFR-9NJpPJY7esVliwsK7gU8ikSTdLO9NNZqDur9-0U1R8EJ9yk3zn3Hs5hDxH-IAA8mNCBggFgCpqwWSxe0AmKIQqgCl8SCbAJC8Yq9UJeZLSDQCyWsjH5AQV1qUo-YQM57ttdCmFrn1PF0MMPljTH26mXdLZtYnG9i6Gu8Mr7Tydu22u-5DoGf0e4pDo5RC9sY5O2z6sXJvo2_lZmq7e0dDSH86kni6CvQ6GLnLdxZCekkferJN7djxPydWn82-zeXHx9fOX2fSisHm6vmgQxbIRzgo0wkovVFU20oJsGsC68nUJ4GrgDRNcKQl-iQosr41YKlFWkp-SN6PvNna3g0u93oRk3XptWtcNSVeyrDj8B8iQCYFiD776C7zphtjmJTQqiZi9WIZwhGzsUorO620MGxN_agS9T06PyemcnN4np3dZ8-JoPDQbt_ytOEaVgddHwCRr1j6a1ob0i2MoBROHVdjIpfzVrlz8Y8J_dH85irzptFnliPTVZYY4YCW4QMXvARC5uIE</recordid><startdate>20090801</startdate><enddate>20090801</enddate><creator>Liu, Rushi</creator><creator>Lin, Qinlu</creator><creator>Sun, Yi</creator><creator>Lu, Xiangyang</creator><creator>Qiu, Yilan</creator><creator>Li, Ye</creator><creator>Guo, Xiangrong</creator><general>New York : Humana Press Inc</general><general>Humana Press Inc</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</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>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</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>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7QO</scope><scope>7U9</scope><scope>H94</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20090801</creationdate><title>Expression, Purification, and Characterization of Hepatitis B Virus Surface Antigens (HBsAg) in Yeast Pichia Pastoris</title><author>Liu, Rushi ; Lin, Qinlu ; Sun, Yi ; Lu, Xiangyang ; Qiu, Yilan ; Li, Ye ; Guo, Xiangrong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-b115db5ec51a5c7f5964b7c07bb0186f8400e803b2539970fd190c38a5d954673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Bioreactors</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Hepatitis</topic><topic>Hepatitis B Surface Antigens - biosynthesis</topic><topic>Hepatitis B Surface Antigens - genetics</topic><topic>Hepatitis B Surface Antigens - immunology</topic><topic>Hepatitis B Surface Antigens - isolation & purification</topic><topic>Hepatitis B virus</topic><topic>Immunization</topic><topic>Immunogenicity</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Pichia - genetics</topic><topic>Pichia - metabolism</topic><topic>Pichia pastoris</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Saccharomyces cerevisiae</topic><topic>Ultracentrifugation</topic><topic>Vaccines</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Rushi</creatorcontrib><creatorcontrib>Lin, Qinlu</creatorcontrib><creatorcontrib>Sun, Yi</creatorcontrib><creatorcontrib>Lu, Xiangyang</creatorcontrib><creatorcontrib>Qiu, Yilan</creatorcontrib><creatorcontrib>Li, Ye</creatorcontrib><creatorcontrib>Guo, Xiangrong</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Rushi</au><au>Lin, Qinlu</au><au>Sun, Yi</au><au>Lu, Xiangyang</au><au>Qiu, Yilan</au><au>Li, Ye</au><au>Guo, Xiangrong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression, Purification, and Characterization of Hepatitis B Virus Surface Antigens (HBsAg) in Yeast Pichia Pastoris</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2009-08-01</date><risdate>2009</risdate><volume>158</volume><issue>2</issue><spage>432</spage><epage>444</epage><pages>432-444</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>Prevention of the prevalence of HB depends upon the development of efficient diagnostic reagent and preventive vaccine. Pichia pastoris offers many advantages over the other expression systems in the production of recombinant HBsAg. In this study, we reported that the recombinant P. pastoris strains were cultured in shake flasks and then scaled up in a 5.0-l bioreactor: approximately 27 mg/l of the protein and the maximal cell OD at 600 nm of 310 were achieved in the bioreactor. The recombinant HBsAg was purified by three steps of purification procedures. SDS-PAGE showed that the purified recombinant HBsAg constituted only one homogeneous band of ~24 kDa. CsCl density gradient ultracentrifugation assay indicated that the density of the HBsAg was 1.2 mg/ml, which was in agreement with the natural HBsAg, the HBsAg expressed in Saccharomyces cerevisiae and in mammalian cells. Electron microscope observation revealed that the purified recombinant HBsAg was homogeneous 22-nm particles, suggesting the HBsAg expressed in P. pastoris was self-assembled to virus-like structures. Competitive ELISA indicated that P. pastoris-derived HBsAg possessed the excellent immunoreaction with anti-HBsAg. Animal immunization showed that the immunogenicity of P. pastoris-derived HBsAg was superior to that of S. cerevisiae-derived HBsAg. Together, our results demonstrated that the recombinant HBsAg expressed in P. pastoris could provide promising, inexpensive, and large-scale materials for the diagnostic reagent and vaccine to prevent HBV infection.</abstract><cop>New York</cop><pub>New York : Humana Press Inc</pub><pmid>19184543</pmid><doi>10.1007/s12010-009-8527-x</doi><tpages>13</tpages></addata></record> |
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| subjects | Animals Biochemistry Biological and medical sciences Bioreactors Biotechnology Chemistry Chemistry and Materials Science Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Female Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Fungal Hepatitis Hepatitis B Surface Antigens - biosynthesis Hepatitis B Surface Antigens - genetics Hepatitis B Surface Antigens - immunology Hepatitis B Surface Antigens - isolation & purification Hepatitis B virus Immunization Immunogenicity Mice Mice, Inbred BALB C Pichia - genetics Pichia - metabolism Pichia pastoris Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - isolation & purification Saccharomyces cerevisiae Ultracentrifugation Vaccines Yeast Yeasts |
| title | Expression, Purification, and Characterization of Hepatitis B Virus Surface Antigens (HBsAg) in Yeast Pichia Pastoris |
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