Simple production of hydrophobin-fused domain III of dengue envelope protein and induction of neutralizing antibodies against the homotypic serotype of dengue virus
Hydrophobin-fused domain III of dengue envelope proteins serotypes 1 and 2 were expressed in Rachiplusia nu larvae and purified by aqueous two-phase system. This biotechnological approach of hydrophobin-fused proteins, which allowed obtaining 97.7 µg/larva of fusion protein DomIII serotype 1 and 61....
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| Veröffentlicht in: | Biotechnology letters 2020-03, Vol.42 (3), p.419-428 |
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| creator | Cerezo, Julieta Targovnik, Alexandra Marisa Smith, María Emilia González Maglio, Daniel Luppo, Victoria Celina Morales, María Alejandra Miranda, María Victoria Rodríguez Talou, Julián |
| description | Hydrophobin-fused domain III of dengue envelope proteins serotypes 1 and 2 were expressed in
Rachiplusia nu
larvae and purified by aqueous two-phase system. This biotechnological approach of hydrophobin-fused proteins, which allowed obtaining 97.7 µg/larva of fusion protein DomIII serotype 1 and 61.4 µg/larva of fusion protein DomIII serotype 2, represents an integrated strategy for simple production of recombinant antigens. Purified fusion proteins induced serotype-specific neutralizing antibodies without cross-reaction against other serotypes and arboviruses after mouse immunization. hydrophobin-fused domain III of dengue envelope protein could be a promising strategy for easy and low-cost production of components of a tetravalent sub-unit vaccine against dengue. |
| doi_str_mv | 10.1007/s10529-019-02767-2 |
| format | Article |
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Rachiplusia nu
larvae and purified by aqueous two-phase system. This biotechnological approach of hydrophobin-fused proteins, which allowed obtaining 97.7 µg/larva of fusion protein DomIII serotype 1 and 61.4 µg/larva of fusion protein DomIII serotype 2, represents an integrated strategy for simple production of recombinant antigens. Purified fusion proteins induced serotype-specific neutralizing antibodies without cross-reaction against other serotypes and arboviruses after mouse immunization. hydrophobin-fused domain III of dengue envelope protein could be a promising strategy for easy and low-cost production of components of a tetravalent sub-unit vaccine against dengue.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-019-02767-2</identifier><identifier>PMID: 31828570</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Antibodies ; Antigens ; Applied Microbiology ; Binary systems ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Cross-reaction ; Dengue fever ; Fusion protein ; Hydrophobins ; Immunization ; Larvae ; Life Sciences ; Microbiology ; Neutralizing ; Original Research Paper ; Proteins ; Serotypes ; Vector-borne diseases ; Viral diseases ; Viral envelope proteins ; Viruses</subject><ispartof>Biotechnology letters, 2020-03, Vol.42 (3), p.419-428</ispartof><rights>Springer Nature B.V. 2019</rights><rights>Biotechnology Letters is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-e41478ba495ee0978f9d60c0ec66aa76ec5a141aa711d6e285f63f8b3d4df2303</citedby><cites>FETCH-LOGICAL-c412t-e41478ba495ee0978f9d60c0ec66aa76ec5a141aa711d6e285f63f8b3d4df2303</cites><orcidid>0000-0003-0006-9908</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-019-02767-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-019-02767-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31828570$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cerezo, Julieta</creatorcontrib><creatorcontrib>Targovnik, Alexandra Marisa</creatorcontrib><creatorcontrib>Smith, María Emilia</creatorcontrib><creatorcontrib>González Maglio, Daniel</creatorcontrib><creatorcontrib>Luppo, Victoria Celina</creatorcontrib><creatorcontrib>Morales, María Alejandra</creatorcontrib><creatorcontrib>Miranda, María Victoria</creatorcontrib><creatorcontrib>Rodríguez Talou, Julián</creatorcontrib><title>Simple production of hydrophobin-fused domain III of dengue envelope protein and induction of neutralizing antibodies against the homotypic serotype of dengue virus</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>Hydrophobin-fused domain III of dengue envelope proteins serotypes 1 and 2 were expressed in
Rachiplusia nu
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Purified fusion proteins induced serotype-specific neutralizing antibodies without cross-reaction against other serotypes and arboviruses after mouse immunization. hydrophobin-fused domain III of dengue envelope protein could be a promising strategy for easy and low-cost production of components of a tetravalent sub-unit vaccine against dengue.</description><subject>Antibodies</subject><subject>Antigens</subject><subject>Applied Microbiology</subject><subject>Binary systems</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cross-reaction</subject><subject>Dengue fever</subject><subject>Fusion protein</subject><subject>Hydrophobins</subject><subject>Immunization</subject><subject>Larvae</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Neutralizing</subject><subject>Original Research Paper</subject><subject>Proteins</subject><subject>Serotypes</subject><subject>Vector-borne 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Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cerezo, Julieta</au><au>Targovnik, Alexandra Marisa</au><au>Smith, María Emilia</au><au>González Maglio, Daniel</au><au>Luppo, Victoria Celina</au><au>Morales, María Alejandra</au><au>Miranda, María Victoria</au><au>Rodríguez Talou, Julián</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Simple production of hydrophobin-fused domain III of dengue envelope protein and induction of neutralizing antibodies against the homotypic serotype of dengue virus</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2020-03-01</date><risdate>2020</risdate><volume>42</volume><issue>3</issue><spage>419</spage><epage>428</epage><pages>419-428</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>Hydrophobin-fused domain III of dengue envelope proteins serotypes 1 and 2 were expressed in
Rachiplusia nu
larvae and purified by aqueous two-phase system. This biotechnological approach of hydrophobin-fused proteins, which allowed obtaining 97.7 µg/larva of fusion protein DomIII serotype 1 and 61.4 µg/larva of fusion protein DomIII serotype 2, represents an integrated strategy for simple production of recombinant antigens. Purified fusion proteins induced serotype-specific neutralizing antibodies without cross-reaction against other serotypes and arboviruses after mouse immunization. hydrophobin-fused domain III of dengue envelope protein could be a promising strategy for easy and low-cost production of components of a tetravalent sub-unit vaccine against dengue.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>31828570</pmid><doi>10.1007/s10529-019-02767-2</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-0006-9908</orcidid></addata></record> |
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| ispartof | Biotechnology letters, 2020-03, Vol.42 (3), p.419-428 |
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| subjects | Antibodies Antigens Applied Microbiology Binary systems Biochemistry Biomedical and Life Sciences Biotechnology Cross-reaction Dengue fever Fusion protein Hydrophobins Immunization Larvae Life Sciences Microbiology Neutralizing Original Research Paper Proteins Serotypes Vector-borne diseases Viral diseases Viral envelope proteins Viruses |
| title | Simple production of hydrophobin-fused domain III of dengue envelope protein and induction of neutralizing antibodies against the homotypic serotype of dengue virus |
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