Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs
Identifieur interne : 000127 ( Pmc/Curation ); précédent : 000126; suivant : 000128Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs
Auteurs : Canping Huang [République populaire de Chine] ; Jianxun Qi [République populaire de Chine] ; Guangwen Lu [République populaire de Chine] ; Qihui Wang [République populaire de Chine] ; Yuan Yuan [République populaire de Chine] ; Ying Wu [République populaire de Chine] ; Yanfang Zhang [République populaire de Chine] ; Jinghua Yan [République populaire de Chine] ; George F. Gao [République populaire de Chine]Source :
- Biochemistry [ 0006-2960 ] ; 2016.
Abstract
The suggested bat origin for Middle East respiratory syndrome coronavirus (MERS-CoV) has revitalized the studies of other bat-derived coronaviruses with respect to interspecies transmission potential. Bat coronavirus (BatCoV) HKU9 is an important betacoronavirus (betaCoV) that is phylogenetically affiliated with the same genus as MERS-CoV. The bat surveillance data indicated that BatCoV HKU9 has been widely spreading and circulating in bats. This highlights the necessity of characterizing the virus for its potential to cross species barriers. The receptor binding domain (RBD) of the coronavirus spike (S) protein recognizes host receptors to mediate virus entry and is therefore a key factor determining the viral tropism and transmission capacity. In this study, the putative S RBD of BatCoV HKU9 (HKU9-RBD), which is homologous to other betaCoV RBDs that have been structurally and functionally defined, was characterized via a series of biophysical and crystallographic methods. By using surface plasmon resonance, we demonstrated that HKU9-RBD binds to neither SARS-CoV receptor ACE2 nor MERS-CoV receptor CD26. We further determined the atomic structure of HKU9-RBD, which as expected is composed of a core and an external subdomain. The core subdomain fold resembles those of other betaCoV RBDs, whereas the external subdomain is structurally unique with a single helix, explaining the inability of HKU9-RBD to react with either ACE2 or CD26. Via comparison of the available RBD structures, we further proposed a homologous intersubdomain binding mode in betaCoV RBDs that anchors the external subdomain to the core subdomain. The revealed RBD features would shed light on the evolution route of betaCoV.
Url:
DOI: 10.1021/acs.biochem.6b00790
PubMed: 27696819
PubMed Central: 7075523
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, Hefei, Anhui Province 230026,<country>China</country>
</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff6">Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology,<institution>Chinese Academy of Sciences</institution>
, Tianjin 300308,<country>China</country>
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<country xml:lang="fr">République populaire de Chine</country>
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<series><title level="j">Biochemistry</title>
<idno type="ISSN">0006-2960</idno>
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<front><div type="abstract" xml:lang="en"><p content-type="toc-graphic"><graphic xlink:href="bi6b00790_0007" id="ab-tgr1"></graphic>
</p>
<p>The suggested bat origin for Middle
East respiratory syndrome coronavirus
(MERS-CoV) has revitalized the studies of other bat-derived coronaviruses
with respect to interspecies transmission potential. Bat coronavirus
(BatCoV) HKU9 is an important betacoronavirus (betaCoV) that is phylogenetically
affiliated with the same genus as MERS-CoV. The bat surveillance data
indicated that BatCoV HKU9 has been widely spreading and circulating
in bats. This highlights the necessity of characterizing the virus
for its potential to cross species barriers. The receptor binding
domain (RBD) of the coronavirus spike (S) protein recognizes host
receptors to mediate virus entry and is therefore a key factor determining
the viral tropism and transmission capacity. In this study, the putative
S RBD of BatCoV HKU9 (HKU9-RBD), which is homologous to other betaCoV
RBDs that have been structurally and functionally defined, was characterized
via a series of biophysical and crystallographic methods. By using
surface plasmon resonance, we demonstrated that HKU9-RBD binds to
neither SARS-CoV receptor ACE2 nor MERS-CoV receptor CD26. We further
determined the atomic structure of HKU9-RBD, which as expected is
composed of a core and an external subdomain. The core subdomain fold
resembles those of other betaCoV RBDs, whereas the external subdomain
is structurally unique with a single helix, explaining the inability
of HKU9-RBD to react with either ACE2 or CD26. Via comparison of the
available RBD structures, we further proposed a homologous intersubdomain
binding mode in betaCoV RBDs that anchors the external subdomain to
the core subdomain. The revealed RBD features would shed light on
the evolution route of betaCoV.</p>
</div>
</front>
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<pmc article-type="research-article" xml:lang="EN"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochemistry</journal-id>
<journal-id journal-id-type="iso-abbrev">Biochemistry</journal-id>
<journal-id journal-id-type="publisher-id">bi</journal-id>
<journal-id journal-id-type="coden">bichaw</journal-id>
<journal-title-group><journal-title>Biochemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0006-2960</issn>
<issn pub-type="epub">1520-4995</issn>
<publisher><publisher-name>American
Chemical Society</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">27696819</article-id>
<article-id pub-id-type="pmc">7075523</article-id>
<article-id pub-id-type="doi">10.1021/acs.biochem.6b00790</article-id>
<article-categories><subj-group><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Putative Receptor Binding Domain of Bat-Derived Coronavirus
HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding
Motifs</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" id="ath1"><name><surname>Huang</surname>
<given-names>Canping</given-names>
</name>
<xref rid="aff1" ref-type="aff">†</xref>
</contrib>
<contrib contrib-type="author" id="ath2"><name><surname>Qi</surname>
<given-names>Jianxun</given-names>
</name>
<xref rid="aff2" ref-type="aff">‡</xref>
</contrib>
<contrib contrib-type="author" id="ath3"><name><surname>Lu</surname>
<given-names>Guangwen</given-names>
</name>
<xref rid="aff3" ref-type="aff">§</xref>
</contrib>
<contrib contrib-type="author" id="ath4"><name><surname>Wang</surname>
<given-names>Qihui</given-names>
</name>
<xref rid="aff4" ref-type="aff">∥</xref>
</contrib>
<contrib contrib-type="author" id="ath5"><name><surname>Yuan</surname>
<given-names>Yuan</given-names>
</name>
<xref rid="aff5" ref-type="aff">⊥</xref>
</contrib>
<contrib contrib-type="author" id="ath6"><name><surname>Wu</surname>
<given-names>Ying</given-names>
</name>
<xref rid="aff2" ref-type="aff">‡</xref>
</contrib>
<contrib contrib-type="author" id="ath7"><name><surname>Zhang</surname>
<given-names>Yanfang</given-names>
</name>
<xref rid="aff2" ref-type="aff">‡</xref>
</contrib>
<contrib contrib-type="author" id="ath8"><name><surname>Yan</surname>
<given-names>Jinghua</given-names>
</name>
<xref rid="aff4" ref-type="aff">∥</xref>
</contrib>
<contrib contrib-type="author" corresp="yes" id="ath9"><name><surname>Gao</surname>
<given-names>George F.</given-names>
</name>
<xref rid="cor1" ref-type="other">*</xref>
<xref rid="aff1" ref-type="aff">†</xref>
<xref rid="aff2" ref-type="aff">‡</xref>
<xref rid="aff5" ref-type="aff">⊥</xref>
<xref rid="aff6" ref-type="aff">#</xref>
<xref rid="aff7" ref-type="aff">@</xref>
</contrib>
<aff id="aff1"><label>†</label>
National Institute for Viral Disease Control and Prevention,<institution>Chinese Center for Disease Control and Prevention (China CDC)</institution>
, Beijing 102206,<country>China</country>
</aff>
<aff id="aff2"><label>‡</label>
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology,<institution>Chinese Academy of Sciences</institution>
, Beijing 100101,<country>China</country>
</aff>
<aff id="aff3"><label>§</label>
West China Hospital Emergency Department (WCHED), State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy, Chengdu, Sichuan 610041,<country>China</country>
</aff>
<aff id="aff4"><label>∥</label>
CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology,<institution>Chinese Academy of Sciences</institution>
, Beijing 100101,<country>China</country>
</aff>
<aff id="aff5"><label>⊥</label>
School of Life Sciences,<institution>University of Science and Technology of China</institution>
, Hefei, Anhui Province 230026,<country>China</country>
</aff>
<aff id="aff6"><label>#</label>
Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Industrial Biotechnology,<institution>Chinese Academy of Sciences</institution>
, Tianjin 300308,<country>China</country>
</aff>
<aff id="aff7"><label>@</label>
Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science,<institution>Chinese Academy of Sciences</institution>
, Beijing 100101,<country>China</country>
</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>*</label>
Telephone: <phone>86-10-64807688</phone>
. Fax: <fax>86-10-64807882</fax>
. E-mail: <email>gaof@im.ac.cn</email>
or <email>gaofu@chinacdc.cn</email>
.</corresp>
</author-notes>
<pub-date pub-type="epub"><day>03</day>
<month>10</month>
<year>2016</year>
</pub-date>
<pub-date pub-type="ppub"><day>01</day>
<month>11</month>
<year>2016</year>
</pub-date>
<volume>55</volume>
<issue>43</issue>
<fpage>5977</fpage>
<lpage>5988</lpage>
<history><date date-type="received"><day>02</day>
<month>08</month>
<year>2016</year>
</date>
<date date-type="rev-recd"><day>26</day>
<month>09</month>
<year>2016</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2016 American Chemical
Society</copyright-statement>
<copyright-year>2016</copyright-year>
<copyright-holder>American Chemical
Society</copyright-holder>
<license license-type="open-access"><license-p>This article is made available via the PMC Open Access Subset 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 the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.</license-p>
</license>
</permissions>
<abstract><p content-type="toc-graphic"><graphic xlink:href="bi6b00790_0007" id="ab-tgr1"></graphic>
</p>
<p>The suggested bat origin for Middle
East respiratory syndrome coronavirus
(MERS-CoV) has revitalized the studies of other bat-derived coronaviruses
with respect to interspecies transmission potential. Bat coronavirus
(BatCoV) HKU9 is an important betacoronavirus (betaCoV) that is phylogenetically
affiliated with the same genus as MERS-CoV. The bat surveillance data
indicated that BatCoV HKU9 has been widely spreading and circulating
in bats. This highlights the necessity of characterizing the virus
for its potential to cross species barriers. The receptor binding
domain (RBD) of the coronavirus spike (S) protein recognizes host
receptors to mediate virus entry and is therefore a key factor determining
the viral tropism and transmission capacity. In this study, the putative
S RBD of BatCoV HKU9 (HKU9-RBD), which is homologous to other betaCoV
RBDs that have been structurally and functionally defined, was characterized
via a series of biophysical and crystallographic methods. By using
surface plasmon resonance, we demonstrated that HKU9-RBD binds to
neither SARS-CoV receptor ACE2 nor MERS-CoV receptor CD26. We further
determined the atomic structure of HKU9-RBD, which as expected is
composed of a core and an external subdomain. The core subdomain fold
resembles those of other betaCoV RBDs, whereas the external subdomain
is structurally unique with a single helix, explaining the inability
of HKU9-RBD to react with either ACE2 or CD26. Via comparison of the
available RBD structures, we further proposed a homologous intersubdomain
binding mode in betaCoV RBDs that anchors the external subdomain to
the core subdomain. The revealed RBD features would shed light on
the evolution route of betaCoV.</p>
</abstract>
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<notes id="notes-d1e21-autogenerated"><fn-group><fn fn-type="" id="d30e240"><p>This article is made available for a limited time sponsored by ACS under the <ext-link ext-link-type="uri" xlink:href="http://pubs.acs.org/page/policy/freetoread/index.html">ACS Free to Read License</ext-link>
, which permits copying and redistribution of the article for non-commercial scholarly purposes.</p>
</fn>
</fn-group>
</notes>
</front>
</pmc>
</record>
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