Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
Identifieur interne : 001441 ( Pmc/Curation ); précédent : 001440; suivant : 001442Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
Auteurs : Yusen Zhou [République populaire de Chine] ; Yang Yang ; Jingwei Huang ; Shibo Jiang ; Lanying DuSource :
- Viruses [ 1999-4915 ] ; 2019.
Abstract
Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) of the S protein contains a critical neutralizing domain and is an important target for development of MERS vaccines and therapeutics. In this review, we describe the relevant features of the MERS-CoV S-protein RBD, summarize recent advances in the development of MERS-CoV RBD-based vaccines and therapeutic antibodies, and illustrate potential challenges and strategies to further improve their efficacy.
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DOI: 10.3390/v11010060
PubMed: 30646569
PubMed Central: 6357101
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain</title><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation><nlm:aff id="af1-viruses-11-00060">State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China;<email>yszhou@bmi.ac.cn</email></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2-viruses-11-00060">Institute of Medical and Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450052, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Medical and Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450052</wicri:regionArea></affiliation></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name><affiliation><nlm:aff id="af3-viruses-11-00060">Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;<email>y.yang@yale.edu</email></nlm:aff></affiliation></author><author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">30646569</idno><idno type="pmc">6357101</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6357101</idno><idno type="RBID">PMC:6357101</idno><idno type="doi">10.3390/v11010060</idno><date when="2019">2019</date><idno type="wicri:Area/Pmc/Corpus">001441</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001441</idno><idno type="wicri:Area/Pmc/Curation">001441</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001441</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain</title><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation><nlm:aff id="af1-viruses-11-00060">State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China;<email>yszhou@bmi.ac.cn</email></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="af2-viruses-11-00060">Institute of Medical and Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450052, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Medical and Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450052</wicri:regionArea></affiliation></author><author><name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name><affiliation><nlm:aff id="af3-viruses-11-00060">Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;<email>y.yang@yale.edu</email></nlm:aff></affiliation></author><author><name sortKey="Huang, Jingwei" sort="Huang, Jingwei" uniqKey="Huang J" first="Jingwei" last="Huang">Jingwei Huang</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation><nlm:aff id="af4-viruses-11-00060">Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</nlm:aff></affiliation></author></analytic><series><title level="j">Viruses</title><idno type="eISSN">1999-4915</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) of the S protein contains a critical neutralizing domain and is an important target for development of MERS vaccines and therapeutics. In this review, we describe the relevant features of the MERS-CoV S-protein RBD, summarize recent advances in the development of MERS-CoV RBD-based vaccines and therapeutic antibodies, and illustrate potential challenges and strategies to further improve their efficacy.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Zaki, A M" uniqKey="Zaki A">A.M. Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S. van Boheemen</name></author><author><name sortKey="Bestebroer, T M" uniqKey="Bestebroer T">T.M. Bestebroer</name></author><author><name sortKey="Osterhaus, A D" uniqKey="Osterhaus A">A.D. Osterhaus</name></author><author><name sortKey="Fouchier, R A" uniqKey="Fouchier R">R.A. Fouchier</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sha, J" uniqKey="Sha J">J. Sha</name></author><author><name sortKey="Li, Y" uniqKey="Li Y">Y. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Viruses</journal-id><journal-id journal-id-type="iso-abbrev">Viruses</journal-id><journal-id journal-id-type="publisher-id">viruses</journal-id><journal-title-group><journal-title>Viruses</journal-title></journal-title-group><issn pub-type="epub">1999-4915</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">30646569</article-id><article-id pub-id-type="pmc">6357101</article-id><article-id pub-id-type="doi">10.3390/v11010060</article-id><article-id pub-id-type="publisher-id">viruses-11-00060</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Zhou</surname><given-names>Yusen</given-names></name><xref ref-type="aff" rid="af1-viruses-11-00060">1</xref><xref ref-type="aff" rid="af2-viruses-11-00060">2</xref></contrib><contrib contrib-type="author"><name><surname>Yang</surname><given-names>Yang</given-names></name><xref ref-type="aff" rid="af3-viruses-11-00060">3</xref></contrib><contrib contrib-type="author"><name><surname>Huang</surname><given-names>Jingwei</given-names></name><xref ref-type="aff" rid="af4-viruses-11-00060">4</xref></contrib><contrib contrib-type="author"><name><surname>Jiang</surname><given-names>Shibo</given-names></name><xref ref-type="aff" rid="af4-viruses-11-00060">4</xref></contrib><contrib contrib-type="author"><name><surname>Du</surname><given-names>Lanying</given-names></name><xref ref-type="aff" rid="af4-viruses-11-00060">4</xref><xref rid="c1-viruses-11-00060" ref-type="corresp">*</xref></contrib></contrib-group><aff id="af1-viruses-11-00060"><label>1</label>State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China;<email>yszhou@bmi.ac.cn</email></aff><aff id="af2-viruses-11-00060"><label>2</label>Institute of Medical and Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450052, China</aff><aff id="af3-viruses-11-00060"><label>3</label>Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;<email>y.yang@yale.edu</email></aff><aff id="af4-viruses-11-00060"><label>4</label>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USA;<email>JHuang2@nybc.org</email> (J.H.);<email>SJiang@nybc.org</email> (S.J.)</aff><author-notes><corresp id="c1-viruses-11-00060"><label>*</label>Correspondence: <email>ldu@nybc.org</email>; Tel.: +1-212-570-3459</corresp></author-notes><pub-date pub-type="epub"><day>14</day><month>1</month><year>2019</year></pub-date><pub-date pub-type="collection"><month>1</month><year>2019</year></pub-date><volume>11</volume><issue>1</issue><elocation-id>60</elocation-id><history><date date-type="received"><day>15</day><month>12</month><year>2018</year></date><date date-type="accepted"><day>10</day><month>1</month><year>2019</year></date></history><permissions><copyright-statement>© 2019 by the authors.</copyright-statement><copyright-year>2019</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><p>Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) of the S protein contains a critical neutralizing domain and is an important target for development of MERS vaccines and therapeutics. In this review, we describe the relevant features of the MERS-CoV S-protein RBD, summarize recent advances in the development of MERS-CoV RBD-based vaccines and therapeutic antibodies, and illustrate potential challenges and strategies to further improve their efficacy.</p></abstract><kwd-group><kwd>Coronavirus</kwd><kwd>MERS-CoV</kwd><kwd>spike protein</kwd><kwd>receptor-binding domain</kwd><kwd>vaccines</kwd><kwd>therapeutics</kwd></kwd-group></article-meta></front><floats-group><fig id="viruses-11-00060-f001" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Schematic structures of MERS-CoV S protein. (<bold>A</bold>) MERS-CoV genomic structure, with the untranslated region (UTR), open reading frame regions ORF1a and ORF1b, spike (S), envelope (E), membrane (M), and nucleocapsid (N) genes. (<bold>B</bold>) Schematic structure of the MERS-CoV virion and its major structural proteins. (<bold>C</bold>) Schematic structure of the MERS-CoV S protein and its functional domains, including the N-terminal domain (NTD), receptor-binding domain (RBD), receptor-binding motif (RBM), fusion peptide (FP), heptad repeat region 1 and 2 (HR1 and HR2), transmembrane region (TM), and cytoplasmic tail (CP). aa, amino acid; MERS-CoV, Middle East respiratory syndrome coronavirus; nt, nucleotide.</p></caption><graphic xlink:href="viruses-11-00060-g001"></graphic></fig><fig id="viruses-11-00060-f002" orientation="portrait" position="float"><label>Figure 2</label><caption><p>Structural basis of MERS-CoV S-protein RBD–DPP4 interaction. Structural data for the complex of MERS-CoV S-protein RBD bound to DPP4 are from the protein data bank (PDB) (ID: 4KR0). The MERS-CoV RBD core is colored in blue, the RBM is colored in red, and DPP4 is colored in green. The RBM residues directly involved in DPP4 binding are shown as sticks. DPP4, dipeptidyl peptidase 4; RBD, receptor-binding domain; RBM, receptor-binding motif; S, spike protein.</p></caption><graphic xlink:href="viruses-11-00060-g002"></graphic></fig><fig id="viruses-11-00060-f003" orientation="portrait" position="float"><label>Figure 3</label><caption><p>Models of the MERS-CoV S-protein trimer bound to DPP4. The models were generated by superimposing the MERS-CoV RBD in the structure of the MERS-CoV S-protein RBD–DPP4 complex (PDB ID: 4KR0) onto the RBDs in the structures of MERS-CoV S-protein trimers with (<bold>A</bold>) one RBD (PDB ID: 5X5F), (<bold>B</bold>) two RBDs (PDB ID: 5X5C), or (<bold>C</bold>) three RBDs (PDB ID: 5X59) in the “standing” conformation. The MERS-CoV S-protein trimers are colored in gray, with three RBDs colored in red, blue, and green. Three DPP4 dimers are colored in plum, orange, and yellow. DPP4, dipeptidyl peptidase 4; PDB, protein data bank; RBD, receptor-binding domain; S, spike protein.</p></caption><graphic xlink:href="viruses-11-00060-g003"></graphic></fig><fig id="viruses-11-00060-f004" orientation="portrait" position="float"><label>Figure 4</label><caption><p>Structural basis for MERS-CoV RBD recognition by neutralizing mAbs. (<bold>A</bold>) Crystal structure of MERS-CoV RBD complexed with MCA1 mAb (PDB ID: 5GMQ). (<bold>B</bold>) Crystal structure of the MERS-CoV RBD complexed with CDC2-C2 mAb (PDB ID: 6C6Z). (<bold>C</bold>) Crystal structure of the MERS-CoV RBD complexed with JC57-14 mAb (PDB ID: 6C6Y). (<bold>D</bold>) Crystal structure of MERS-CoV RBD complexed with MERS-4 mAb (PDB ID: 5ZXV). The MERS-CoV RBD core is colored in blue, the RBM is colored in red, and the heavy chains and light chains of each mAb are colored in green and yellow, respectively. The DPP4-binding residues that are blocked by each mAb are shown as sticks. mAb, monoclonal antibody; MERS-CoV, Middle East respiratory syndrome coronavirus; PDB, protein data bank; RBD, receptor-binding domain; RBM, receptor-binding motif.</p></caption><graphic xlink:href="viruses-11-00060-g004"></graphic></fig><table-wrap id="viruses-11-00060-t001" orientation="portrait" position="float"><object-id pub-id-type="pii">viruses-11-00060-t001_Table 1</object-id><label>Table 1</label><caption><p>Vaccines based on MERS-CoV RBD. Live MERS-CoV strains used for neutralization and challenge experiments, as well as vaccine-induced neutralizing-antibody titers, are described in parentheses.</p></caption><table frame="hsides" rules="groups"><thead><tr><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Name</th><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Functionality and Antigenicity</th><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Immunogenicity in Induction of Antibody Response</th><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Immunogenicity in Induction of Cellular Immune Response</th><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Protective Immunity</th><th valign="top" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Ref. </th></tr></thead><tbody><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">RBD-[SSG]-FR and RBD-FR nanoparticles</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Bind to DPP4 receptor; antisera block RBD-hDPP4 binding</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induce MERS-CoV RBD-specific antibodies (IgG, IgG1, IgG2a, IgG2b, IgA) in mice</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Elicit MERS-CoV RBD-specific T-cell responses (IFN-γ, TNF-α) in mouse splenocytes</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B89-viruses-11-00060" ref-type="bibr">89</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">sVLP <break></break>(spherical virus-like particle)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induces MERS-CoV RBD-specific antibodies (IgG) in mice, neutralizing pseudotyped MERS-CoV (1:320)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Elicits MERS-CoV RBD-specific cellular immune response (IFN-γ, IL-2, IL-4) in mouse splenocytes </td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B90-viruses-11-00060" ref-type="bibr">90</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">rRBD (recombinant RBD)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induces MERS-CoV RBD-specific antibodies (IgG, IgG1, IgG2a) in mice or NHPs, neutralizing pseudotyped (1:800 to 1:1,600) and live (EMC2012: 1:269 to 1:363) MERS-CoV</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Elicits MERS-CoV RBD-specific cellular immune response (TNF-α, IFN-γ, IL-2, IL-4, IL-6) in mouse splenocytes or monkey PBMCs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Partially protects NHPs from MERS-CoV (EMC2012: 6.5 × 10<sup>7</sup> TCID<sub>50</sub>) infection with alleviated pneumonia and decreased viral load</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B88-viruses-11-00060" ref-type="bibr">88</xref>,<xref rid="B91-viruses-11-00060" ref-type="bibr">91</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">RBD<break></break>(S377-588)-Fc</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Binds strongly to soluble and cell-associated hDPP4 or cDPP4 receptors and MERS-CoV RBD-specific neutralizing mAbs (Mersmab1, m336, m337, m338)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induces MERS-CoV S1-specific antibodies (IgG, IgG1, IgG2a) in mice and rabbits, cross-neutralizing 17 pseudotyped (>1:10<sup>4</sup>), 2 live (EMC2012, London1-2012: ≥1:10<sup>3</sup>) MERS-CoV, and 5 mAb escape mutants (>1:10<sup>4</sup>)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Elicits MERS-CoV S1-specific cellular immune responses (IFN-γ, IL-2) in mouse splenocytes</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Protects Ad5/hDPP4-transduced BALB/c mice and hDPP4-Tg mice (67% survival rate) from challenge by MERS-CoV (EMC2012: 10<sup>5</sup> PFU for BALB/c; 10<sup>3–</sup>10<sup>4</sup> TCID<sub>50</sub> for Tg), without toxicity or immune enhancement</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B92-viruses-11-00060" ref-type="bibr">92</xref>,<xref rid="B95-viruses-11-00060" ref-type="bibr">95</xref>,<xref rid="B96-viruses-11-00060" ref-type="bibr">96</xref>,<xref rid="B97-viruses-11-00060" ref-type="bibr">97</xref>,<xref rid="B98-viruses-11-00060" ref-type="bibr">98</xref>,<xref rid="B99-viruses-11-00060" ref-type="bibr">99</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">2012-RBD<break></break>2013-RBD<break></break>2014-RBD<break></break>2015-RBD<break></break>Camel-RBD</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Bind strongly to hDPP4 and cDPP4 receptors and MERS-CoV RBD-specific mAbs (Mersmab1, m336, m337, m338) with high affinity</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induce MERS-CoV S1-specific antibodies (IgG, IgG1, IgG2a) in mice, potently cross-neutralizing 17 pseudotyped (≥1:10<sup>4</sup>), 2 live (EMC2012, London1-2012: >1:10<sup>2</sup>) MERS-CoV, and 5 mAb escape mutants (≥1:10<sup>4</sup>)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B100-viruses-11-00060" ref-type="bibr">100</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">RBD-Fd</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Binds strongly to soluble and cell-associated hDPP4 receptors and MERS-CoV RBD-specific mAbs (Mersmab1, m336, m337, m338)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induces robust and long-term MERS-CoV S1-specific antibodies (IgG, IgG1, IgG2a) in mice, neutralizing at least 9 pseudotyped (>1:10<sup>4</sup>) and live (EMC2012: >1:10<sup>3</sup>) MERS-CoV</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Protects hDPP4-Tg mice (83% survival rate) from lethal MERS-CoV (EMC2012: 10<sup>4</sup> TCID<sub>50</sub>) challenge </td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B94-viruses-11-00060" ref-type="bibr">94</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">RBD (T579N)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Binds strongly to soluble and cell-associated hDPP4 receptors and MERS-CoV RBD-specific mAbs (hHS-1, m336, m337, m338)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Induces highly potent neutralizing antibodies in mice against live MERS-CoV (EMC2012: >1:3 × 10<sup>3</sup>)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Significantly enhances efficacy in fully protecting hDPP4-Tg mice (100% survival rate) from lethal MERS-CoV (EMC2012: 10<sup>4</sup> TCID<sub>50</sub>) challenge</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B93-viruses-11-00060" ref-type="bibr">93</xref>]</td></tr></tbody></table><table-wrap-foot><fn><p>Note: Ad5, adenovirus 5; DPP4, dipeptidyl peptidase 4; cDPP4, camel DPP4; hDPP4, human DPP4; hDPP4-Tg, hDPP4-transgenic; Fd, foldon; FR, ferritin; mAb, monoclonal antibody; N/A, not available or not applicable; NHP, non-human primate; PBMCs, peripheral blood mononuclear cells; PFU, plaque-forming unit; RBD, receptor-binding domain; S, spike; TCID<sub>50</sub>, median tissue-culture infectious dose.</p></fn></table-wrap-foot></table-wrap><table-wrap id="viruses-11-00060-t002" orientation="portrait" position="float"><object-id pub-id-type="pii">viruses-11-00060-t002_Table 2</object-id><label>Table 2</label><caption><p>Therapeutic antibodies targeting MERS-CoV RBD. Live MERS-CoV strains used for neutralization and challenge experiments are indicated in parentheses.</p></caption><table frame="hsides" rules="groups"><thead><tr><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Name</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Source</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Binding MERS-CoV RBD</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Structure Available</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">In vitro Anti-MERS-CoV Activity</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">In vivo Protection</th><th valign="middle" align="left" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Ref.</th></tr></thead><tbody><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">MERS-GD27 MERS-GD33 mAbs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Human</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>K</italic><sub>d</sub>: 0.775 nM (for MERS-GD27) and 0.575 nM (for MERS-GD33). Recognize RBD residues L506, D510, E513, W535, E536, D539, E540, W553 (for MERS-GD27), R511, and A556 (for MERS-GD33)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Yes, crystal structure for the Fab–RBD complex</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">IC<sub>50</sub>: 0.001 µg/mL against pseudotyped MERS-CoV; 0.001 µg/mL against live MERS-CoV; both mAbs have synergistic effect against pseudotyped MERS-CoV with reduced IC<sub>50</sub> by 0.499-fold (for MERS-GD27) or 6.05-fold (for MERS-GD33) vs individual mAbs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">MERS-GD27 prophylactically and therapeutically protects hDPP4-Tg mice against MERS-CoV (EMC2012: 3 LD<sub>50</sub>) with 60% and 40% survival rates, respectively</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B112-viruses-11-00060" ref-type="bibr">112</xref>,<xref rid="B113-viruses-11-00060" ref-type="bibr">113</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">MCA1 <break></break>mAb</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Human</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Recognizes RBD residues D510, W535, E536, D539, Y540, R542, and Q544</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Yes, crystal structure for the Fab–RBD complex</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">IC<sub>50</sub>: 0.39 µg/mL against live MERS-CoV (EMC2012) </td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Prophylactically and therapeutically (5–20 mg/kg) inhibits MERS-CoV (EMC2012: 5 × 10<sup>6</sup> TCID<sub>50</sub>) replication in common marmosets, improving clinical outcomes and reducing lung disease and viral replication</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B114-viruses-11-00060" ref-type="bibr">114</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">JC57-14 <break></break>mAb</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Macaque</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Recognizes RBD residues W535, E536, D539, Y540, and R542</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Yes, crystal structure for the Fab–RBD complex</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">IC<sub>50</sub>: 0.0084 µg/mL against pseudotyped MERS-CoV and 0.07 µg/mL against live MERS-CoV (EMC2012), cross-neutralizing 8 pseudotyped MERS-CoVs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B102-viruses-11-00060" ref-type="bibr">102</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">CDC2-C2 mAb</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Human</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Recognizes RBD residues F506, D509, W535, E536, D539, Y540, and R542</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Yes, crystal structure for the Fab–RBD complex</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">IC<sub>50</sub>: 0.0057 µg/mL against pseudotyped MERS-CoV and 0.058 µg/mL against live MERS-CoV (EMC2012), cross-neutralizing 10 pseudotyped MERS-CoVs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Prophylactically (20 mg/kg) protects hDPP4-Tg mice against MERS-CoV (EMC2012: 10<sup>6</sup> TCID<sub>50</sub>) in lungs with 100% survival rate</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B102-viruses-11-00060" ref-type="bibr">102</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">MERS-4 <break></break>mAb</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Human</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Recognizes RBD residues L507, L545, S546, P547, G549; binds RBD from outside of the RBD DPP4-binding interface</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Yes, crystal structure for the Fab–RBD complex</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Has synergistic neutralization effect with MERS-27, m336, and 5F9 mAbs against pseudotyped MERS-CoV, with the reduction of IC<sub>50</sub> by 2.6-fold (for MERS-4 + m336) and 15.21-fold (for MERS-4 + 5F9)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B115-viruses-11-00060" ref-type="bibr">115</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">VHH-83<break></break>HCAb-83 <break></break>VHHs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Dromedary</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>K</italic><sub>d</sub>: 0.1 nM (for VHH-83) and 2.5 pM (for HCAb-83). Recognizes RBD residue D539</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">PRNT<sub>50</sub>: 0.0012–0.0014 µg/mL against live MERS-CoV (EMC2012)</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">HCAb-83 (200 µg) prophylactically protects hDPP4-Tg mice (K18) against MERS-CoV (EMC2012: 10<sup>5</sup> PFU) in lungs with 100% survival rate</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B116-viruses-11-00060" ref-type="bibr">116</xref>]</td></tr><tr><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">NbMS10<break></break>NbMS10-Fc <break></break>VHHs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">Llama</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1"><italic>K</italic><sub>d</sub>: 0.87 nM (for NbMS10) and 0.35 nM (for NbMS10-Fc). Recognize RBD residue D539</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">N/A</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">IC<sub>50</sub>: 0.003–0.979 µg/ml (for NbMS10) and 0.003–0.067 µg/ml (for NbMS10-Fc) in cross-neutralizing ≥11 pseudotyped MERS-CoVs</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">NbMS10-Fc (10 mg/kg) prophylactically and therapeutically protects hDPP4-Tg mice against MERS-CoV (EMC2012, 10<sup>5.3</sup> TCID<sub>50</sub>) with 100% survival rate</td><td valign="top" align="left" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B117-viruses-11-00060" ref-type="bibr">117</xref>]</td></tr></tbody></table><table-wrap-foot><fn><p>Note: DPP4, dipeptidyl peptidase 4; Fab, antigen-binding fragment; hDPP4-Tg, human DPP4-transgenic; IC<sub>50</sub>, half-maximal inhibitory concentration; <italic>K</italic><sub>d</sub>: antibody binding affinity; LD<sub>50</sub>, 50% lethal dose; N/A, not available or not applicable; PRNT<sub>50</sub>, 50% plaque-reduction neutralization titer; RBD, receptor-binding domain; TCID<sub>50</sub>, median tissue-culture infectious dose; VHH, single-domain antibody fragment.</p></fn></table-wrap-foot></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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