A recombinant receptor-binding domain of MERS-CoV in trimeric form protects human dipeptidyl peptidase 4 (hDPP4) transgenic mice from MERS-CoV infection
Identifieur interne : 000744 ( Pmc/Curation ); précédent : 000743; suivant : 000745A recombinant receptor-binding domain of MERS-CoV in trimeric form protects human dipeptidyl peptidase 4 (hDPP4) transgenic mice from MERS-CoV infection
Auteurs : Wanbo Tai [République populaire de Chine, États-Unis] ; Guangyu Zhao [République populaire de Chine] ; Shihun Sun [République populaire de Chine] ; Yan Guo [République populaire de Chine] ; Yufei Wang [République populaire de Chine, États-Unis] ; Xinrong Tao [États-Unis] ; Chien-Te K. Tseng [États-Unis] ; Fang Li [États-Unis] ; Shibo Jiang [États-Unis, République populaire de Chine] ; Lanying Du [États-Unis] ; Yusen Zhou [République populaire de Chine]Source :
- Virology [ 0042-6822 ] ; 2016.
Abstract
Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) was first identified in 2012, and it continues to threaten human health worldwide. No MERS vaccines are licensed for human use, reinforcing the urgency to develop safe and efficacious vaccines to prevent MERS. MERS-CoV spike protein forms a trimer, and its receptor-binding domain (RBD) serves as a vaccine target. Nevertheless, the protective efficacy of RBD in its native trimeric form has never been evaluated. In this study, a trimeric protein, RBD-Fd, was generated by fusing RBD with foldon trimerization motif. It bound strongly to the receptor of MERS-CoV, dipeptidyl peptidase 4 (DPP4), and elicited robust RBD-specific neutralizing antibodies in mice, maintaining long-term neutralizing activity against MERS-CoV infection. RBD-Fd potently protected hDPP4 transgenic mice from lethal MERS-CoV challenge. These results suggest that MERS-CoV RBD in its trimeric form maintains native conformation and induces protective neutralizing antibodies, making it a candidate for further therapeutic development.
Url:
DOI: 10.1016/j.virol.2016.10.005
PubMed: 27750111
PubMed Central: 5167628
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<front><div type="abstract" xml:lang="en"><p>Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) was first identified in 2012, and it continues to threaten human health worldwide. No MERS vaccines are licensed for human use, reinforcing the urgency to develop safe and efficacious vaccines to prevent MERS. MERS-CoV spike protein forms a trimer, and its receptor-binding domain (RBD) serves as a vaccine target. Nevertheless, the protective efficacy of RBD in its native trimeric form has never been evaluated. In this study, a trimeric protein, RBD-Fd, was generated by fusing RBD with foldon trimerization motif. It bound strongly to the receptor of MERS-CoV, dipeptidyl peptidase 4 (DPP4), and elicited robust RBD-specific neutralizing antibodies in mice, maintaining long-term neutralizing activity against MERS-CoV infection. RBD-Fd potently protected hDPP4 transgenic mice from lethal MERS-CoV challenge. These results suggest that MERS-CoV RBD in its trimeric form maintains native conformation and induces protective neutralizing antibodies, making it a candidate for further therapeutic development.</p>
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</TEI>
<pmc article-type="brief-report"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Virology</journal-id>
<journal-id journal-id-type="iso-abbrev">Virology</journal-id>
<journal-title-group><journal-title>Virology</journal-title>
</journal-title-group>
<issn pub-type="ppub">0042-6822</issn>
<issn pub-type="epub">1096-0341</issn>
<publisher><publisher-name>Elsevier Inc.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27750111</article-id>
<article-id pub-id-type="pmc">5167628</article-id>
<article-id pub-id-type="publisher-id">S0042-6822(16)30300-2</article-id>
<article-id pub-id-type="doi">10.1016/j.virol.2016.10.005</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>A recombinant receptor-binding domain of MERS-CoV in trimeric form protects human dipeptidyl peptidase 4 (hDPP4) transgenic mice from MERS-CoV infection</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Tai</surname>
<given-names>Wanbo</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author" id="au0010"><name><surname>Zhao</surname>
<given-names>Guangyu</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0015"><name><surname>Sun</surname>
<given-names>Shihun</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0020"><name><surname>Guo</surname>
<given-names>Yan</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0025"><name><surname>Wang</surname>
<given-names>Yufei</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author" id="au0030"><name><surname>Tao</surname>
<given-names>Xinrong</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author" id="au0035"><name><surname>Tseng</surname>
<given-names>Chien-Te K.</given-names>
</name>
<xref rid="aff0015" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author" id="au0040"><name><surname>Li</surname>
<given-names>Fang</given-names>
</name>
<xref rid="aff0020" ref-type="aff">d</xref>
</contrib>
<contrib contrib-type="author" id="au0045"><name><surname>Jiang</surname>
<given-names>Shibo</given-names>
</name>
<email>sjiang@nybc.org</email>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="aff0025" ref-type="aff">e</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
<contrib contrib-type="author" id="au0050"><name><surname>Du</surname>
<given-names>Lanying,</given-names>
</name>
<email>ldu@nybc.org</email>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="cor2" ref-type="corresp">⁎⁎</xref>
</contrib>
<contrib contrib-type="author" id="au0055"><name><surname>Zhou</surname>
<given-names>Yusen</given-names>
</name>
<email>yszhou@bmi.ac.cn</email>
<xref rid="aff0005" ref-type="aff">a</xref>
<xref rid="cor2" ref-type="corresp">⁎⁎</xref>
</contrib>
</contrib-group>
<aff id="aff0005"><label>a</label>
State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China</aff>
<aff id="aff0010"><label>b</label>
Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA</aff>
<aff id="aff0015"><label>c</label>
Department of Microbiology and Immunology and Center for Biodefense and Emerging Disease, University of Texas Medical Branch, Galveston, TX, USA</aff>
<aff id="aff0020"><label>d</label>
Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN, USA</aff>
<aff id="aff0025"><label>e</label>
Key Laboratory of Medical Molecular Virology of Ministries of Education and Health, Basic Medical College and Institute of Medical Microbiology, Fudan University, Shanghai, China</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Corresponding author at: Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. <email>sjiang@nybc.org</email>
</corresp>
<corresp id="cor2"><label>⁎⁎</label>
Corresponding authors. <email>ldu@nybc.org</email>
<email>yszhou@bmi.ac.cn</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release"><day>15</day>
<month>10</month>
<year>2016</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"><month>12</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="epub"><day>15</day>
<month>10</month>
<year>2016</year>
</pub-date>
<volume>499</volume>
<fpage>375</fpage>
<lpage>382</lpage>
<history><date date-type="received"><day>18</day>
<month>7</month>
<year>2016</year>
</date>
<date date-type="rev-recd"><day>4</day>
<month>10</month>
<year>2016</year>
</date>
<date date-type="accepted"><day>6</day>
<month>10</month>
<year>2016</year>
</date>
</history>
<permissions><copyright-statement>© 2016 Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2016</copyright-year>
<copyright-holder>Elsevier Inc.</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 id="ab0010"><p>Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) was first identified in 2012, and it continues to threaten human health worldwide. No MERS vaccines are licensed for human use, reinforcing the urgency to develop safe and efficacious vaccines to prevent MERS. MERS-CoV spike protein forms a trimer, and its receptor-binding domain (RBD) serves as a vaccine target. Nevertheless, the protective efficacy of RBD in its native trimeric form has never been evaluated. In this study, a trimeric protein, RBD-Fd, was generated by fusing RBD with foldon trimerization motif. It bound strongly to the receptor of MERS-CoV, dipeptidyl peptidase 4 (DPP4), and elicited robust RBD-specific neutralizing antibodies in mice, maintaining long-term neutralizing activity against MERS-CoV infection. RBD-Fd potently protected hDPP4 transgenic mice from lethal MERS-CoV challenge. These results suggest that MERS-CoV RBD in its trimeric form maintains native conformation and induces protective neutralizing antibodies, making it a candidate for further therapeutic development.</p>
</abstract>
<abstract abstract-type="graphical" id="ab0015"><title>Graphical abstract</title>
<p><fig id="f0025" position="anchor"><alt-text id="at0025">fx1</alt-text>
<graphic xlink:href="fx1_lrg"></graphic>
</fig>
</p>
</abstract>
<abstract abstract-type="author-highlights" id="ab0020"><title>Highlights</title>
<p><list list-type="simple" id="li0005"><list-item id="u0005"><label>•</label>
<p id="p0005">A trimeric MERS-CoV protein (RBD-Fd) was constructed by fusing viral RBD with foldon trimerization motif.</p>
</list-item>
<list-item id="u0010"><label>•</label>
<p id="p0010">RBD-Fd bound strongly to dipeptidyl peptidase 4 (DPP4), the receptor of MERS-CoV, and RBD-specific neutralizing antibodies.</p>
</list-item>
<list-item id="u0015"><label>•</label>
<p id="p0015">RBD-Fd induced robust and long-term neutralizing antibodies, cross-neutralizing MERS pseudovirus of divergent strains.</p>
</list-item>
<list-item id="u0020"><label>•</label>
<p id="p0020">RBD-Fd potently protected hDPP4 transgenic mice from lethal MERS-CoV challenge.</p>
</list-item>
</list>
</p>
</abstract>
<kwd-group id="keys0005"><title>Keywords</title>
<kwd>MERS</kwd>
<kwd>MERS-CoV</kwd>
<kwd>Spike protein</kwd>
<kwd>Receptor-binding domain</kwd>
<kwd>Foldon trimerization motif</kwd>
<kwd>Neutralization</kwd>
<kwd>hDPP4-transgenic mice</kwd>
<kwd>Protection</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>
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