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Receptor-binding domains of spike proteins of emerging or re-emerging viruses as targets for development of antiviral vaccines

Identifieur interne : 000A37 ( Pmc/Checkpoint ); précédent : 000A36; suivant : 000A38

Receptor-binding domains of spike proteins of emerging or re-emerging viruses as targets for development of antiviral vaccines

Auteurs : Shibo Jiang [République populaire de Chine, États-Unis] ; Lu Lu [République populaire de Chine] ; Qi Liu [République populaire de Chine] ; Wei Xu [République populaire de Chine] ; Lanying Du [États-Unis]

Source :

RBID : PMC:3630917

Abstract

A number of emerging and re-emerging viruses have caused epidemics or pandemics of infectious diseases leading to major devastations throughout human history. Therefore, developing effective and safe vaccines against these viruses is clearly important for the protection of at-risk populations. Our previous studies have shown that the receptor-binding domain (RBD) in the spike protein of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) is a key target for the development of SARS vaccines. In this review, we highlight some key advances in the development of antiviral vaccines targeting the RBDs of spike proteins of emerging and re-emerging viruses, using SARS-CoV, influenza virus, Hendra virus (HeV) and Nipah virus (NiV) as examples.


Url:
DOI: 10.1038/emi.2012.1
PubMed: 26038424
PubMed Central: 3630917


Affiliations:


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PMC:3630917

Le document en format XML

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</back>
</TEI>
<pmc article-type="review-article">
<pmc-dir>properties open_access</pmc-dir>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Emerg Microbes Infect</journal-id>
<journal-id journal-id-type="iso-abbrev">Emerg Microbes Infect</journal-id>
<journal-title-group>
<journal-title>Emerging Microbes & Infections</journal-title>
</journal-title-group>
<issn pub-type="epub">2222-1751</issn>
<publisher>
<publisher-name>Nature Publishing Group</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">26038424</article-id>
<article-id pub-id-type="pmc">3630917</article-id>
<article-id pub-id-type="pii">emi20121</article-id>
<article-id pub-id-type="doi">10.1038/emi.2012.1</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Review</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Receptor-binding domains of spike proteins of emerging or re-emerging viruses as targets for development of antiviral vaccines</article-title>
<alt-title alt-title-type="running">Receptor-binding domains-based antiviral vaccines</alt-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Jiang</surname>
<given-names>Shibo</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff2">2</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Lu</surname>
<given-names>Lu</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Liu</surname>
<given-names>Qi</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="aff" rid="aff3">3</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Xu</surname>
<given-names>Wei</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Du</surname>
<given-names>Lanying</given-names>
</name>
<xref ref-type="aff" rid="aff2">2</xref>
</contrib>
<aff id="aff1">
<label>1</label>
<institution>MOE/MOH Key Laboratory of Medical Molecular Virology, Shanghai Medical College and Institute of Medical Microbiology, Fudan University</institution>
, Shanghai 200032,
<country>China</country>
</aff>
<aff id="aff2">
<label>2</label>
<institution>Lindsley F. Kimball Research Institute, New York Blood Center</institution>
, New York, NY 10065,
<country>USA</country>
</aff>
<aff id="aff3">
<label>3</label>
<institution>Department of Medical Microbiology and Immunology, School of Basic Medicine, Dali University</institution>
, Dali 671000,
<country>China</country>
</aff>
</contrib-group>
<author-notes>
<corresp id="caf1">
<label>*</label>
E-mail:
<email>shibojiang@fudan.edu.cn</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub">
<month>08</month>
<year>2012</year>
</pub-date>
<pub-date pub-type="epub">
<day>08</day>
<month>08</month>
<year>2012</year>
</pub-date>
<pub-date pub-type="pmc-release">
<day>1</day>
<month>8</month>
<year>2012</year>
</pub-date>
<volume>1</volume>
<issue>8</issue>
<fpage>e13</fpage>
<lpage></lpage>
<history>
<date date-type="received">
<day>07</day>
<month>03</month>
<year>2012</year>
</date>
<date date-type="rev-recd">
<day>10</day>
<month>03</month>
<year>2012</year>
</date>
<date date-type="accepted">
<day>12</day>
<month>03</month>
<year>2012</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright © 2012 Shanghai Shangyixun Cultural Communication Co., Ltd</copyright-statement>
<copyright-year>2012</copyright-year>
<copyright-holder>Shanghai Shangyixun Cultural Communication Co., Ltd</copyright-holder>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by-nc-nd/3.0/">
<pmc-comment>author-paid</pmc-comment>
<license-p>This work is licensed under the Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/</license-p>
</license>
</permissions>
<abstract>
<p>A number of emerging and re-emerging viruses have caused epidemics or pandemics of infectious diseases leading to major devastations throughout human history. Therefore, developing effective and safe vaccines against these viruses is clearly important for the protection of at-risk populations. Our previous studies have shown that the receptor-binding domain (RBD) in the spike protein of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) is a key target for the development of SARS vaccines. In this review, we highlight some key advances in the development of antiviral vaccines targeting the RBDs of spike proteins of emerging and re-emerging viruses, using SARS-CoV, influenza virus, Hendra virus (HeV) and Nipah virus (NiV) as examples.</p>
</abstract>
<kwd-group>
<kwd>Hendra virus</kwd>
<kwd>influenza virus</kwd>
<kwd>Nipah virus</kwd>
<kwd>receptor-binding domain</kwd>
<kwd>SARS-CoV</kwd>
<kwd>spike protein</kwd>
<kwd>vaccine</kwd>
<kwd>virus</kwd>
</kwd-group>
</article-meta>
</front>
<floats-group>
<fig id="fig1">
<label>Figure 1</label>
<caption>
<p>The interaction between the receptor-binding domain in the spike of an emerging virus and the corresponding receptor on the target cell.</p>
</caption>
<graphic xlink:href="emi20121f1"></graphic>
</fig>
<fig id="fig2">
<label>Figure 2</label>
<caption>
<p>The RBDs in the envelope glycoproteins of SARS-CoV, influenza virus and Hendra virus. (
<bold>A</bold>
) RBD in the SARS-CoV spike protein.
<sup>
<xref ref-type="bibr" rid="bib14">14</xref>
,
<xref ref-type="bibr" rid="bib17">17</xref>
,
<xref ref-type="bibr" rid="bib79">79</xref>
</sup>
The residue numbers of each region represent their positions in the S protein of SARS-CoV. (
<bold>B</bold>
) RBD in influenza virus HA. Taking H5N1 as an example, HA consists of a globular ‘head' HA1 subunit containing the receptor-binding domain RBD and a membrane proximal HA2 subunit with α-helical stalk region (FP). The leading sequence (SP) is located at the N-terminus of HA1. There is a protease cleavage site between HA1 and HA2 subunits characterized by specific amino acid sequences, e.g., RERRRKKR. HA1 and HA2 subunits were connected by interchain disulfide bond from HA1-aa14 to HA2-aa137.
<sup>
<xref ref-type="bibr" rid="bib80">80</xref>
</sup>
(
<bold>C</bold>
) RBD in the Hendra virus G glycoprotein. There are many glycosylate sites in the extracellular domain located in 72, 159, 306, 378, 417, 481 and 529, respectively. Residues from aa 439 to aa 468, which are located in RBD domain, are an important domain within G for receptor interaction. CP, cytoplasm domain; EC, extracellular domain; FP, fusion peptide; HA, hemagglutinin; HR, heptad repeat; RBM, receptor-binding motif; TM, transmembrane domain; SP, signal peptide.</p>
</caption>
<graphic xlink:href="emi20121f2"></graphic>
</fig>
<fig id="fig3">
<label>Figure 3</label>
<caption>
<p>The SARS-CoV life cycle in host cells and its S protein structure. Life cycle of SARS-CoV. SARS-CoV begins its life cycle when its S protein binds to the cellular receptor ACE2. After receptor binding, the conformation change in the S protein facilitates viral envelope fusion with the cell membrane through the endosomal pathway. Then SARS-CoV releases RNA into the host cell. Genome RNA is translated into viral replicase polyproteins pp1a and 1ab, which are then cleaved into small products by viral proteinases. At the same time, polymerase, which produces a series of subgenomic mRNAs by discontinuous transcription, is finally translated into relevant viral proteins. Viral proteins and genome RNA are subsequently assembled into virions in the ER and Golgi, which are budding into the lumen of the ERGIC and then transported via vesicles and released out of the cell. ACE2, angiotensin-converting enzyme 2; ER, endoplasmic reticulum; ERGIC, ER–Golgi intermediate compartment.</p>
</caption>
<graphic xlink:href="emi20121f3"></graphic>
</fig>
<fig id="fig4">
<label>Figure 4</label>
<caption>
<p>The structure and natural reservoirs of HeV. The principal natural reservoirs for HeV are fruit bats. Recent evidence of Hendra infection has indicated that flying foxes can also be natural reservoirs. The secondary vectors can be laboratory rodents, cats, dogs and rabbits. The dead-end hosts are horse and man. HeV has six major structural proteins. They are nucleocapsid protein (N), phosphorprotein (P), matrix protein (M), fusion protein (F), glycoprotein (G) and large protein (L). HeV, Hendra virus.</p>
</caption>
<graphic xlink:href="emi20121f4"></graphic>
</fig>
</floats-group>
</pmc>
<affiliations>
<list>
<country>
<li>République populaire de Chine</li>
<li>États-Unis</li>
</country>
</list>
<tree>
<country name="République populaire de Chine">
<noRegion>
<name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
</noRegion>
<name sortKey="Liu, Qi" sort="Liu, Qi" uniqKey="Liu Q" first="Qi" last="Liu">Qi Liu</name>
<name sortKey="Liu, Qi" sort="Liu, Qi" uniqKey="Liu Q" first="Qi" last="Liu">Qi Liu</name>
<name sortKey="Lu, Lu" sort="Lu, Lu" uniqKey="Lu L" first="Lu" last="Lu">Lu Lu</name>
<name sortKey="Xu, Wei" sort="Xu, Wei" uniqKey="Xu W" first="Wei" last="Xu">Wei Xu</name>
</country>
<country name="États-Unis">
<noRegion>
<name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name>
</noRegion>
<name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name>
</country>
</tree>
</affiliations>
</record>

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