Searching for an ideal vaccine candidate among different MERS coronavirus receptor-binding fragments—The importance of immunofocusing in subunit vaccine design
Identifieur interne : 001165 ( Pmc/Curation ); précédent : 001164; suivant : 001166Searching for an ideal vaccine candidate among different MERS coronavirus receptor-binding fragments—The importance of immunofocusing in subunit vaccine design
Auteurs : Cuiqing Ma [États-Unis] ; Lili Wang [États-Unis] ; Xinrong Tao [États-Unis] ; Naru Zhang [États-Unis] ; Yang Yang [États-Unis] ; Chien-Te K. Tseng [États-Unis] ; Fang Li [États-Unis] ; Yusen Zhou [République populaire de Chine] ; Shibo Jiang [États-Unis, République populaire de Chine] ; Lanying Du [États-Unis]Source :
- Vaccine [ 0264-410X ] ; 2014.
Abstract
We express five MERS-CoV RBDs spanning S350-588, 358-588, 367-588, 377-606, and 377-588. S377-588, 367-588 and 358-588 have the highest receptor binding ability than others. S377-588 and 367-588 induced the highest-titer of IgG antibodies in mice. S377-588 elicits highest neutralization in mice and high neutralization in rabbits. S377-588 contains stably folded RBD structure and major neutralizing epitopes.
Url:
DOI: 10.1016/j.vaccine.2014.08.086
PubMed: 25240756
PubMed Central: 4194190
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Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff0025">Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai</wicri:regionArea></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25240756</idno><idno type="pmc">4194190</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4194190</idno><idno type="RBID">PMC:4194190</idno><idno type="doi">10.1016/j.vaccine.2014.08.086</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">001165</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001165</idno><idno type="wicri:Area/Pmc/Curation">001165</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001165</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Searching for an ideal vaccine candidate among different MERS coronavirus receptor-binding fragments—The importance of immunofocusing in subunit vaccine design</title><author><name sortKey="Ma, Cuiqing" sort="Ma, Cuiqing" uniqKey="Ma C" first="Cuiqing" last="Ma">Cuiqing Ma</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation></author><author><name sortKey="Wang, Lili" sort="Wang, Lili" uniqKey="Wang L" first="Lili" last="Wang">Lili Wang</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation></author><author><name sortKey="Tao, Xinrong" sort="Tao, Xinrong" uniqKey="Tao X" first="Xinrong" last="Tao">Xinrong Tao</name><affiliation wicri:level="1"><nlm:aff id="aff0010">Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX</wicri:regionArea></affiliation></author><author><name sortKey="Zhang, Naru" sort="Zhang, Naru" uniqKey="Zhang N" first="Naru" last="Zhang">Naru Zhang</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name><affiliation wicri:level="1"><nlm:aff id="aff0015">Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN</wicri:regionArea></affiliation></author><author><name sortKey="Tseng, Chien Te K" sort="Tseng, Chien Te K" uniqKey="Tseng C" first="Chien-Te K" last="Tseng">Chien-Te K. Tseng</name><affiliation wicri:level="1"><nlm:aff id="aff0010">Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX</wicri:regionArea></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation wicri:level="1"><nlm:aff id="aff0015">Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN</wicri:regionArea></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation wicri:level="1"><nlm:aff id="aff0020">State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing</wicri:regionArea></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff0025">Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai</wicri:regionArea></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation wicri:level="1"><nlm:aff id="aff0005">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY</wicri:regionArea></affiliation></author></analytic><series><title level="j">Vaccine</title><idno type="ISSN">0264-410X</idno><idno type="eISSN">1873-2518</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Highlights</title><p><list list-type="simple" id="lis0005"><list-item id="lsti0005"><label>•</label><p id="par0005">We express five MERS-CoV RBDs spanning S350-588, 358-588, 367-588, 377-606, and 377-588.</p></list-item><list-item id="lsti0010"><label>•</label><p id="par0010">S377-588, 367-588 and 358-588 have the highest receptor binding ability than others.</p></list-item><list-item id="lsti0015"><label>•</label><p id="par0015">S377-588 and 367-588 induced the highest-titer of IgG antibodies in mice.</p></list-item><list-item id="lsti0020"><label>•</label><p id="par0020">S377-588 elicits highest neutralization in mice and high neutralization in rabbits.</p></list-item><list-item id="lsti0025"><label>•</label><p id="par0025">S377-588 contains stably folded RBD structure and major neutralizing epitopes.</p></list-item></list></p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Zaki, A M" uniqKey="Zaki A">A.M. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Vaccine</journal-id><journal-id journal-id-type="iso-abbrev">Vaccine</journal-id><journal-title-group><journal-title>Vaccine</journal-title></journal-title-group><issn pub-type="ppub">0264-410X</issn><issn pub-type="epub">1873-2518</issn><publisher><publisher-name>Elsevier Ltd.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25240756</article-id><article-id pub-id-type="pmc">4194190</article-id><article-id pub-id-type="publisher-id">S0264-410X(14)01255-9</article-id><article-id pub-id-type="doi">10.1016/j.vaccine.2014.08.086</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Searching for an ideal vaccine candidate among different MERS coronavirus receptor-binding fragments—The importance of immunofocusing in subunit vaccine design</article-title></title-group><contrib-group><contrib contrib-type="author" id="aut0005"><name><surname>Ma</surname><given-names>Cuiqing</given-names></name><xref rid="aff0005" ref-type="aff">a</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="aut0010"><name><surname>Wang</surname><given-names>Lili</given-names></name><xref rid="aff0005" ref-type="aff">a</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="aut0015"><name><surname>Tao</surname><given-names>Xinrong</given-names></name><xref rid="aff0010" ref-type="aff">b</xref></contrib><contrib contrib-type="author" id="aut0020"><name><surname>Zhang</surname><given-names>Naru</given-names></name><xref rid="aff0005" ref-type="aff">a</xref></contrib><contrib contrib-type="author" id="aut0025"><name><surname>Yang</surname><given-names>Yang</given-names></name><xref rid="aff0015" ref-type="aff">c</xref></contrib><contrib contrib-type="author" id="aut0030"><name><surname>Tseng</surname><given-names>Chien-Te K</given-names></name><xref rid="aff0010" ref-type="aff">b</xref></contrib><contrib contrib-type="author" id="aut0035"><name><surname>Li</surname><given-names>Fang</given-names></name><xref rid="aff0015" ref-type="aff">c</xref></contrib><contrib contrib-type="author" id="aut0040"><name><surname>Zhou</surname><given-names>Yusen</given-names></name><xref rid="aff0020" ref-type="aff">d</xref></contrib><contrib contrib-type="author" id="aut0045"><name><surname>Jiang</surname><given-names>Shibo</given-names></name><email>sjiang@nybloodcenter.org</email><xref rid="aff0005" ref-type="aff">a</xref><xref rid="aff0025" ref-type="aff">e</xref><xref rid="cor0005" ref-type="corresp">⁎</xref></contrib><contrib contrib-type="author" id="aut0050"><name><surname>Du</surname><given-names>Lanying</given-names></name><email>ldu@nybloodcenter.org</email><xref rid="aff0005" ref-type="aff">a</xref><xref rid="cor0005" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="aff0005"><label>a</label>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</aff><aff id="aff0010"><label>b</label>Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX, USA</aff><aff id="aff0015"><label>c</label>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA</aff><aff id="aff0020"><label>d</label>State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China</aff><aff id="aff0025"><label>e</label>Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Shanghai Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China</aff><author-notes><corresp id="cor0005"><label>⁎</label>Corresponding authors at: New York Blood Center, Viral Immunology, 310 East 67th Street, New York, NY 10021, USA. Tel.: +1 212 570 3058/+1 212 570 3459; fax: +1 212 570 3099/+1 212 570 3299.. <email>sjiang@nybloodcenter.org</email><email>ldu@nybloodcenter.org</email></corresp><fn id="fn1"><label>1</label><p id="npar0005">These authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>19</day><month>9</month><year>2014</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>21</day><month>10</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>19</day><month>9</month><year>2014</year></pub-date><volume>32</volume><issue>46</issue><fpage>6170</fpage><lpage>6176</lpage><history><date date-type="received"><day>25</day><month>5</month><year>2014</year></date><date date-type="rev-recd"><day>20</day><month>7</month><year>2014</year></date><date date-type="accepted"><day>22</day><month>8</month><year>2014</year></date></history><permissions><copyright-statement>Copyright © 2014 Elsevier Ltd. All rights reserved.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>Elsevier Ltd</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract abstract-type="author-highlights" id="abs0005"><title>Highlights</title><p><list list-type="simple" id="lis0005"><list-item id="lsti0005"><label>•</label><p id="par0005">We express five MERS-CoV RBDs spanning S350-588, 358-588, 367-588, 377-606, and 377-588.</p></list-item><list-item id="lsti0010"><label>•</label><p id="par0010">S377-588, 367-588 and 358-588 have the highest receptor binding ability than others.</p></list-item><list-item id="lsti0015"><label>•</label><p id="par0015">S377-588 and 367-588 induced the highest-titer of IgG antibodies in mice.</p></list-item><list-item id="lsti0020"><label>•</label><p id="par0020">S377-588 elicits highest neutralization in mice and high neutralization in rabbits.</p></list-item><list-item id="lsti0025"><label>•</label><p id="par0025">S377-588 contains stably folded RBD structure and major neutralizing epitopes.</p></list-item></list></p></abstract><abstract id="abs0010"><p>The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) is currently spreading among humans, making development of effective MERS vaccines a high priority. A defined receptor-binding domain (RBD) in MERS-CoV spike protein can potentially serve as a subunit vaccine candidate against MERS-CoV infections. To identify an ideal vaccine candidate, we have constructed five different versions of RBD fragments, S350-588-Fc, S358-588-Fc, S367-588-Fc, S367-606-Fc, and S377-588-Fc (their names indicate their residue range in the spike protein and their C-terminal Fc tag), and further investigated their receptor binding affinity, antigenicity, immunogenicity, and neutralizing potential. The results showed that S377-588-Fc is among the RBD fragments that demonstrated the highest DPP4-binding affinity and induced the highest-titer IgG antibodies in mice. In addition, S377-588-Fc elicited higher-titer neutralizing antibodies than all the other RBD fragments in mice, and also induced high-titer neutralizing antibodies in immunized rabbits. Structural analysis suggests that S377-588-Fc contains the stably folded RBD structure, the full receptor-binding site, and major neutralizing epitopes, such that additional structures to this fragment introduce non-neutralizing epitopes and may also alter the tertiary structure of the RBD. Taken together, our data suggest that the RBD fragment encompassing spike residues 377-588 is a critical neutralizing receptor-binding fragment and an ideal candidate for development of effective MERS vaccines, and that adding non-neutralizing structures to this RBD fragment diminishes its neutralizing potential. Therefore, in viral vaccine design, it is important to identify the most stable and neutralizing viral RBD fragment, while eliminating unnecessary and non-neutralizing structures, as a means of “immunofocusing”.</p></abstract><kwd-group id="kwd0005"><title>Keywords</title><kwd>MERS</kwd><kwd>MERS-CoV</kwd><kwd>Spike protein</kwd><kwd>Receptor-binding domain</kwd><kwd>Critical neutralizing domain</kwd><kwd>Immunofocusing</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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