Built-in RNA-mediated Chaperone (Chaperna) for Antigen Folding Tailored to Immunized Hosts.
Identifieur interne : 000286 ( Main/Exploration ); précédent : 000285; suivant : 000287Built-in RNA-mediated Chaperone (Chaperna) for Antigen Folding Tailored to Immunized Hosts.
Auteurs : Young-Seok Kim [Corée du Sud] ; Jongkwan Lim [Corée du Sud] ; Jemin Sung [Corée du Sud] ; Yucheol Cheong [Corée du Sud] ; Eun-Young Lee [Corée du Sud] ; Jihoon Kim [Corée du Sud] ; Hana Oh [Corée du Sud] ; Yeon-Sook Kim [Corée du Sud] ; Nam-Hyuk Cho [Corée du Sud] ; Seongil Choi [Suède] ; Sang-Moo Kang [États-Unis] ; Jae-Hwan Nam [Corée du Sud] ; Wonil Chae [Corée du Sud] ; Baik L. Seong [Corée du Sud]Source :
- Biotechnology and bioengineering [ 1097-0290 ] ; 2020.
Abstract
High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the "self" RID tag remained non-immunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS-CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc-mediated effector function was demonstrated, which could be harnessed for the design of next-generation "universal" influenza vaccines. The non-immunogenic built-in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics and designer vaccines. This article is protected by copyright. All rights reserved.
DOI: 10.1002/bit.27355
PubMed: 32297972
Affiliations:
- Corée du Sud, Suède, États-Unis
- Géorgie (États-Unis), Région capitale de Séoul, Svealand
- Stockholm, Séoul
- Université de Stockholm
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wicri:level="2"><nlm:affiliation>Center for Inflammation, Immunity & Infection, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Inflammation, Immunity & Infection, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA</wicri:regionArea><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation></author><author><name sortKey="Nam, Jae Hwan" sort="Nam, Jae Hwan" uniqKey="Nam J" first="Jae-Hwan" last="Nam">Jae-Hwan Nam</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology, The Catholic University of Korea, Bucheon, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Biotechnology, The Catholic University of Korea, Bucheon</wicri:regionArea><wicri:noRegion>Bucheon</wicri:noRegion></affiliation></author><author><name sortKey="Chae, Wonil" sort="Chae, Wonil" uniqKey="Chae W" first="Wonil" last="Chae">Wonil Chae</name><affiliation wicri:level="3"><nlm:affiliation>Department of Biotechnology, College of Life Sciences and Biotechnology, Yonsei University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Biotechnology, College of Life Sciences and Biotechnology, Yonsei University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName></affiliation></author><author><name sortKey="Seong, Baik L" sort="Seong, Baik L" uniqKey="Seong B" first="Baik L" last="Seong">Baik L. Seong</name><affiliation wicri:level="3"><nlm:affiliation>Department of Biotechnology, College of Life Sciences and Biotechnology, Yonsei University, Seoul, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Biotechnology, College of Life Sciences and Biotechnology, Yonsei University, Seoul</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName></affiliation></author></analytic><series><title level="j">Biotechnology and bioengineering</title><idno type="eISSN">1097-0290</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the "self" RID tag remained non-immunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS-CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc-mediated effector function was demonstrated, which could be harnessed for the design of next-generation "universal" influenza vaccines. The non-immunogenic built-in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics and designer vaccines. This article is protected by copyright. All rights reserved.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li><li>Suède</li><li>États-Unis</li></country><region><li>Géorgie (États-Unis)</li><li>Région capitale de Séoul</li><li>Svealand</li></region><settlement><li>Stockholm</li><li>Séoul</li></settlement><orgName><li>Université de Stockholm</li></orgName></list><tree><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Kim, Young Seok" sort="Kim, Young Seok" uniqKey="Kim Y" first="Young-Seok" last="Kim">Young-Seok Kim</name></region><name sortKey="Chae, Wonil" sort="Chae, Wonil" uniqKey="Chae W" first="Wonil" last="Chae">Wonil Chae</name><name sortKey="Cheong, Yucheol" sort="Cheong, Yucheol" uniqKey="Cheong Y" first="Yucheol" last="Cheong">Yucheol Cheong</name><name sortKey="Cho, Nam Hyuk" sort="Cho, Nam Hyuk" uniqKey="Cho N" first="Nam-Hyuk" last="Cho">Nam-Hyuk Cho</name><name sortKey="Kim, Jihoon" sort="Kim, Jihoon" uniqKey="Kim J" first="Jihoon" last="Kim">Jihoon Kim</name><name sortKey="Kim, Yeon Sook" sort="Kim, Yeon Sook" uniqKey="Kim Y" first="Yeon-Sook" last="Kim">Yeon-Sook Kim</name><name sortKey="Lee, Eun Young" sort="Lee, Eun Young" uniqKey="Lee E" first="Eun-Young" last="Lee">Eun-Young Lee</name><name sortKey="Lim, Jongkwan" sort="Lim, Jongkwan" uniqKey="Lim J" first="Jongkwan" last="Lim">Jongkwan Lim</name><name sortKey="Nam, Jae Hwan" sort="Nam, Jae Hwan" uniqKey="Nam J" first="Jae-Hwan" last="Nam">Jae-Hwan Nam</name><name sortKey="Oh, Hana" sort="Oh, Hana" uniqKey="Oh H" first="Hana" last="Oh">Hana Oh</name><name sortKey="Seong, Baik L" sort="Seong, Baik L" uniqKey="Seong B" first="Baik L" last="Seong">Baik L. Seong</name><name sortKey="Sung, Jemin" sort="Sung, Jemin" uniqKey="Sung J" first="Jemin" last="Sung">Jemin Sung</name></country><country name="Suède"><region name="Svealand"><name sortKey="Choi, Seongil" sort="Choi, Seongil" uniqKey="Choi S" first="Seongil" last="Choi">Seongil Choi</name></region></country><country name="États-Unis"><region name="Géorgie (États-Unis)"><name sortKey="Kang, Sang Moo" sort="Kang, Sang Moo" uniqKey="Kang S" first="Sang-Moo" last="Kang">Sang-Moo Kang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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