Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry
Identifieur interne : 001064 ( Pmc/Checkpoint ); précédent : 001063; suivant : 001065Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry
Auteurs : Wenfei Song [République populaire de Chine] ; Ying Wang [République populaire de Chine] ; Nianshuang Wang [République populaire de Chine] ; Dongli Wang [République populaire de Chine] ; Jianying Guo [République populaire de Chine] ; Lili Fu [République populaire de Chine] ; Xuanling Shi [République populaire de Chine]Source :
- Virology [ 0042-6822 ] ; 2014.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Here, we report identification of critical residues on hDPP4 for RBD binding and virus entry through analysis of a panel of hDPP4 mutants. Based on the RBD–hDPP4 crystal structure we reported, the mutated residues were located at the interface between RBD and hDPP4, which potentially changed the polarity, hydrophobic or hydrophilic properties of hDPP4, thereby interfering or disrupting their interaction with RBD. Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues in hDPP4–RBD binding interface were important on hDPP4–RBD binding and viral entry. These results provide atomic insights into the features of interactions between hDPP4 and MERS-CoV RBD, and also provide potential explanation for cellular and species tropism of MERS-CoV infection.
Url:
DOI: 10.1016/j.virol.2014.10.006
PubMed: 25461530
PubMed Central: 7112127
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Here, we report identification of critical residues on hDPP4 for RBD binding and virus entry through analysis of a panel of hDPP4 mutants. Based on the RBD–hDPP4 crystal structure we reported, the mutated residues were located at the interface between RBD and hDPP4, which potentially changed the polarity, hydrophobic or hydrophilic properties of hDPP4, thereby interfering or disrupting their interaction with RBD. Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues in hDPP4–RBD binding interface were important on hDPP4–RBD binding and viral entry. These results provide atomic insights into the features of interactions between hDPP4 and MERS-CoV RBD, and also provide potential explanation for cellular and species tropism of MERS-CoV infection.</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">25461530</article-id>
<article-id pub-id-type="pmc">7112127</article-id>
<article-id pub-id-type="publisher-id">S0042-6822(14)00453-X</article-id>
<article-id pub-id-type="doi">10.1016/j.virol.2014.10.006</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Identification of residues on human receptor DPP4 critical for MERS-CoV binding and entry</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Song</surname>
<given-names>Wenfei</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="au0010"><name><surname>Wang</surname>
<given-names>Ying</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author" id="au0015"><name><surname>Wang</surname>
<given-names>Nianshuang</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0020"><name><surname>Wang</surname>
<given-names>Dongli</given-names>
</name>
<xref rid="aff0005" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author" id="au0025"><name><surname>Guo</surname>
<given-names>Jianying</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author" id="au0030"><name><surname>Fu</surname>
<given-names>Lili</given-names>
</name>
<xref rid="aff0010" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author" id="au0035"><name><surname>Shi</surname>
<given-names>Xuanling</given-names>
</name>
<email>shixuanlingsk@tsinghua.edu.cn</email>
<xref rid="aff0010" ref-type="aff">b</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
</contrib-group>
<aff id="aff0005"><label>a</label>
Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China</aff>
<aff id="aff0010"><label>b</label>
Comprehensive AIDS Research Center, Research Center for Public Health, School of Medicine, Tsinghua University, Beijing 100084, China</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Corresponding author. Tel.: +86 10 6279 7532. <email>shixuanlingsk@tsinghua.edu.cn</email>
</corresp>
<fn id="fn1"><label>1</label>
<p id="ntp0005">These two authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>21</day>
<month>10</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"><month>12</month>
<year>2014</year>
</pub-date>
<pub-date pub-type="epub"><day>21</day>
<month>10</month>
<year>2014</year>
</pub-date>
<volume>471</volume>
<fpage>49</fpage>
<lpage>53</lpage>
<history><date date-type="received"><day>16</day>
<month>6</month>
<year>2014</year>
</date>
<date date-type="rev-recd"><day>24</day>
<month>9</month>
<year>2014</year>
</date>
<date date-type="accepted"><day>6</day>
<month>10</month>
<year>2014</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2014 Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2014</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="ab0005"><p>Middle East respiratory syndrome coronavirus (MERS-CoV) infects host cells through binding the receptor binding domain (RBD) on its spike glycoprotein to human receptor dipeptidyl peptidase 4 (hDPP4). Here, we report identification of critical residues on hDPP4 for RBD binding and virus entry through analysis of a panel of hDPP4 mutants. Based on the RBD–hDPP4 crystal structure we reported, the mutated residues were located at the interface between RBD and hDPP4, which potentially changed the polarity, hydrophobic or hydrophilic properties of hDPP4, thereby interfering or disrupting their interaction with RBD. Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues in hDPP4–RBD binding interface were important on hDPP4–RBD binding and viral entry. These results provide atomic insights into the features of interactions between hDPP4 and MERS-CoV RBD, and also provide potential explanation for cellular and species tropism of MERS-CoV infection.</p>
</abstract>
<abstract abstract-type="author-highlights" id="ab0410"><title>Highlights</title>
<p><list list-type="simple" id="li0005"><list-item id="u0505"><label>•</label>
<p id="p0405">It has been demonstrated that MERS-CoV infects host cells through binding its envelope spike (S) glycoprotein to the host cellular receptor dipeptidyl peptidase 4 (DPP4).</p>
</list-item>
<list-item id="u0310"><label>•</label>
<p id="p0410">To identify the critical residues on hDPP4 for RBD binding and virus entry, we constructed a panel of hDPP4 mutants based on structure-guided mutagenesis.</p>
</list-item>
<list-item id="u0215"><label>•</label>
<p id="p0515">Using surface plasmon resonance (SPR) binding analysis and pseudovirus infection assay, we showed that several residues on hDPP4 had significant impacts on virus/receptor interactions and viral entry.</p>
</list-item>
<list-item id="u0220"><label>•</label>
<p id="p0420">Our study has provided new insights into the features of interactions between hDPP4 and MERS-CoV RBD, and provides potential explanation for cellular and species tropism of MERS-CoV infection.</p>
</list-item>
</list>
</p>
</abstract>
<kwd-group id="keys0005"><title>Keywords</title>
<kwd>MERS-CoV</kwd>
<kwd>hDPP4</kwd>
<kwd>RBD</kwd>
<kwd>Amino-acid residue substitution</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>République populaire de Chine</li>
</country>
<settlement><li>Pékin</li>
</settlement>
</list>
<tree><country name="République populaire de Chine"><noRegion><name sortKey="Song, Wenfei" sort="Song, Wenfei" uniqKey="Song W" first="Wenfei" last="Song">Wenfei Song</name>
</noRegion>
<name sortKey="Fu, Lili" sort="Fu, Lili" uniqKey="Fu L" first="Lili" last="Fu">Lili Fu</name>
<name sortKey="Guo, Jianying" sort="Guo, Jianying" uniqKey="Guo J" first="Jianying" last="Guo">Jianying Guo</name>
<name sortKey="Shi, Xuanling" sort="Shi, Xuanling" uniqKey="Shi X" first="Xuanling" last="Shi">Xuanling Shi</name>
<name sortKey="Wang, Dongli" sort="Wang, Dongli" uniqKey="Wang D" first="Dongli" last="Wang">Dongli Wang</name>
<name sortKey="Wang, Nianshuang" sort="Wang, Nianshuang" uniqKey="Wang N" first="Nianshuang" last="Wang">Nianshuang Wang</name>
<name sortKey="Wang, Ying" sort="Wang, Ying" uniqKey="Wang Y" first="Ying" last="Wang">Ying Wang</name>
</country>
</tree>
</affiliations>
</record>
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