Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein
We developed a novel surface display system based on the CotB anchoring motif in order to express foreign protein on the surface of vegetative Bacillus subtilis cells. CotB is a protein in the B. subtilis spore coat. In this system, three repeats of the immunodominant ovalbumin T-cell epitope (OVA 3...
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| Veröffentlicht in: | World journal of microbiology & biotechnology 2011-03, Vol.27 (3), p.719-726 |
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| creator | Han, Meimei Enomoto, Keiichi |
| description | We developed a novel surface display system based on the CotB anchoring motif in order to express foreign protein on the surface of vegetative
Bacillus subtilis
cells. CotB is a protein in the
B. subtilis
spore coat. In this system, three repeats of the immunodominant ovalbumin T-cell epitope (OVA
323–339
) were linked with the cholera toxin B subunit (CTB) to construct a fusion protein, CTB-OVA epi, which was then fused to the C-terminal of the CotB protein so that CTB-OVA epi was expressed in vegetatively-growing
B. subtilis
. The expression and localization of the CTB-OVA epi protein was confirmed by western blotting, immunofluorescence microscopy, and flow cytometry. The results indicated that a CotB-based surface display system was successfully used to express the CTB-OVA epi protein on the surface of vegetative
B. subtilis
cells. |
| doi_str_mv | 10.1007/s11274-010-0490-8 |
| format | Article |
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Bacillus subtilis
cells. CotB is a protein in the
B. subtilis
spore coat. In this system, three repeats of the immunodominant ovalbumin T-cell epitope (OVA
323–339
) were linked with the cholera toxin B subunit (CTB) to construct a fusion protein, CTB-OVA epi, which was then fused to the C-terminal of the CotB protein so that CTB-OVA epi was expressed in vegetatively-growing
B. subtilis
. The expression and localization of the CTB-OVA epi protein was confirmed by western blotting, immunofluorescence microscopy, and flow cytometry. The results indicated that a CotB-based surface display system was successfully used to express the CTB-OVA epi protein on the surface of vegetative
B. subtilis
cells.</description><identifier>ISSN: 0959-3993</identifier><identifier>EISSN: 1573-0972</identifier><identifier>DOI: 10.1007/s11274-010-0490-8</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Anchoring ; Anchors ; Antibodies ; Antigens ; Applied Microbiology ; Bacillus subtilis ; Bacteria ; Binding sites ; Biochemistry ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Cholera ; E coli ; Environmental Engineering/Biotechnology ; Flow cytometry ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Genetic engineering ; Gram-negative bacteria ; Gram-positive bacteria ; Life Sciences ; Microbiology ; Microscopy ; Peptides ; Plasmids ; Polyethylene glycol ; Position (location) ; Proteins ; Recombinant ; Short Communication ; Studies ; Tetanus ; Toxins ; Vaccines ; Waterborne diseases</subject><ispartof>World journal of microbiology & biotechnology, 2011-03, Vol.27 (3), p.719-726</ispartof><rights>Springer Science+Business Media B.V. 2010</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media B.V. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-174a7115341cbdb5feff35876f673a7e440b4c02793e9cbc7cde97890f8ee7c63</citedby><cites>FETCH-LOGICAL-c508t-174a7115341cbdb5feff35876f673a7e440b4c02793e9cbc7cde97890f8ee7c63</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/s11274-010-0490-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11274-010-0490-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23876568$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Han, Meimei</creatorcontrib><creatorcontrib>Enomoto, Keiichi</creatorcontrib><title>Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein</title><title>World journal of microbiology & biotechnology</title><addtitle>World J Microbiol Biotechnol</addtitle><description>We developed a novel surface display system based on the CotB anchoring motif in order to express foreign protein on the surface of vegetative
Bacillus subtilis
cells. CotB is a protein in the
B. subtilis
spore coat. In this system, three repeats of the immunodominant ovalbumin T-cell epitope (OVA
323–339
) were linked with the cholera toxin B subunit (CTB) to construct a fusion protein, CTB-OVA epi, which was then fused to the C-terminal of the CotB protein so that CTB-OVA epi was expressed in vegetatively-growing
B. subtilis
. The expression and localization of the CTB-OVA epi protein was confirmed by western blotting, immunofluorescence microscopy, and flow cytometry. The results indicated that a CotB-based surface display system was successfully used to express the CTB-OVA epi protein on the surface of vegetative
B. subtilis
cells.</description><subject>Anchoring</subject><subject>Anchors</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Applied Microbiology</subject><subject>Bacillus subtilis</subject><subject>Bacteria</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cholera</subject><subject>E coli</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Flow cytometry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Genetic engineering</subject><subject>Gram-negative bacteria</subject><subject>Gram-positive bacteria</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Microscopy</subject><subject>Peptides</subject><subject>Plasmids</subject><subject>Polyethylene glycol</subject><subject>Position (location)</subject><subject>Proteins</subject><subject>Recombinant</subject><subject>Short Communication</subject><subject>Studies</subject><subject>Tetanus</subject><subject>Toxins</subject><subject>Vaccines</subject><subject>Waterborne diseases</subject><issn>0959-3993</issn><issn>1573-0972</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kVFrFDEUhYNYcK3-AN-CIPoyejOZzE1eBLvYKhT60PocMtmkm2U2WZOZwv57s-5aUdCnQO53DveeQ8grBu8ZAH4ojLXYNcCggU5BI5-QBRPIG1DYPiULUEI1XCn-jDwvZQMVBMUXZHM7Z2-so6tQdqPZ0-RpdjZthxBNnOgup8mFSFOk09pR68aRlpOkohfGhnGcS_0bpjCGQof9T3CZpgtqol2n_MvjBTnzZizu5ek9J98uP98tvzTXN1dfl5-uGytATg3DziBjgnfMDqtBeOc9FxJ73yM36LoOhs5Ci4o7ZQeLduUUSgVeOoe25-fk49F3Nw9bt7IuTtmMepfD1uS9TiboPycxrPV9etAIUgpsq8Hbk0FO32dXJr0N5XC5iS7NRcu-40oqKSr57r8kQ5SADHlX0dd_oZs051iD0FKwehQHXiF2hGxOpWTnH7dmoA8962PPutanDz1rWTVvTsamWDP6XFMP5VHY8hqd6A9ce-RKHcV7l38v8G_zH5ctuS4</recordid><startdate>20110301</startdate><enddate>20110301</enddate><creator>Han, Meimei</creator><creator>Enomoto, Keiichi</creator><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TB</scope><scope>7TK</scope><scope>7U5</scope><scope>7U9</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>H94</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>L7M</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>7QO</scope><scope>5PM</scope></search><sort><creationdate>20110301</creationdate><title>Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein</title><author>Han, Meimei ; Enomoto, Keiichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-174a7115341cbdb5feff35876f673a7e440b4c02793e9cbc7cde97890f8ee7c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Anchoring</topic><topic>Anchors</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>Applied Microbiology</topic><topic>Bacillus subtilis</topic><topic>Bacteria</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cholera</topic><topic>E coli</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Flow cytometry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Genetic engineering</topic><topic>Gram-negative bacteria</topic><topic>Gram-positive bacteria</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Microscopy</topic><topic>Peptides</topic><topic>Plasmids</topic><topic>Polyethylene glycol</topic><topic>Position (location)</topic><topic>Proteins</topic><topic>Recombinant</topic><topic>Short Communication</topic><topic>Studies</topic><topic>Tetanus</topic><topic>Toxins</topic><topic>Vaccines</topic><topic>Waterborne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Han, Meimei</creatorcontrib><creatorcontrib>Enomoto, Keiichi</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology 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Biotechnol</stitle><date>2011-03-01</date><risdate>2011</risdate><volume>27</volume><issue>3</issue><spage>719</spage><epage>726</epage><pages>719-726</pages><issn>0959-3993</issn><eissn>1573-0972</eissn><abstract>We developed a novel surface display system based on the CotB anchoring motif in order to express foreign protein on the surface of vegetative
Bacillus subtilis
cells. CotB is a protein in the
B. subtilis
spore coat. In this system, three repeats of the immunodominant ovalbumin T-cell epitope (OVA
323–339
) were linked with the cholera toxin B subunit (CTB) to construct a fusion protein, CTB-OVA epi, which was then fused to the C-terminal of the CotB protein so that CTB-OVA epi was expressed in vegetatively-growing
B. subtilis
. The expression and localization of the CTB-OVA epi protein was confirmed by western blotting, immunofluorescence microscopy, and flow cytometry. The results indicated that a CotB-based surface display system was successfully used to express the CTB-OVA epi protein on the surface of vegetative
B. subtilis
cells.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><doi>10.1007/s11274-010-0490-8</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0959-3993 |
| ispartof | World journal of microbiology & biotechnology, 2011-03, Vol.27 (3), p.719-726 |
| issn | 0959-3993 1573-0972 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7088572 |
| source | Springer Nature - Complete Springer Journals |
| subjects | Anchoring Anchors Antibodies Antigens Applied Microbiology Bacillus subtilis Bacteria Binding sites Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnology Cholera E coli Environmental Engineering/Biotechnology Flow cytometry Fundamental and applied biological sciences. Psychology Gene expression Genetic engineering Gram-negative bacteria Gram-positive bacteria Life Sciences Microbiology Microscopy Peptides Plasmids Polyethylene glycol Position (location) Proteins Recombinant Short Communication Studies Tetanus Toxins Vaccines Waterborne diseases |
| title | Surface display of recombinant protein on the cell surface of Bacillus subtilis by the CotB anchor protein |
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