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A novel peptide with potent and broad-spectrum antiviral activities against multiple respiratory viruses

Identifieur interne : 001089 ( Main/Exploration ); précédent : 001088; suivant : 001090

A novel peptide with potent and broad-spectrum antiviral activities against multiple respiratory viruses

Auteurs : Hanjun Zhao [République populaire de Chine] ; Jie Zhou [République populaire de Chine] ; Ke Zhang [République populaire de Chine] ; Hin Chu [République populaire de Chine] ; Dabin Liu [République populaire de Chine] ; Vincent Kwok-Man Poon [République populaire de Chine] ; Chris Chung-Sing Chan [République populaire de Chine] ; Ho-Chuen Leung [République populaire de Chine] ; Ng Fai [République populaire de Chine] ; Yong-Ping Lin [République populaire de Chine] ; Anna Jin-Xia Zhang [République populaire de Chine] ; Dong-Yan Jin [République populaire de Chine] ; Kwok-Yung Yuen [République populaire de Chine] ; Bo-Jian Zheng [République populaire de Chine]

Source :

RBID : PMC:4766503

Descripteurs français

English descriptors

Abstract

A safe, potent and broad-spectrum antiviral is urgently needed to combat emerging respiratory viruses. In light of the broad antiviral activity of β-defensins, we tested the antiviral activity of 11 peptides derived from mouse β-defensin-4 and found that a short peptide, P9, exhibited potent and broad-spectrum antiviral effects against multiple respiratory viruses in vitro and in vivo, including influenza A virus H1N1, H3N2, H5N1, H7N7, H7N9, SARS-CoV and MERS-CoV. The antiviral activity of P9 was attributed to its high-affinity binding to viral glycoproteins, as well as the abundance of basic amino acids in its composition. After binding viral particles through viral surface glycoproteins, P9 entered into cells together with the viruses via endocytosis and prevented endosomal acidification, which blocked membrane fusion and subsequent viral RNA release. This study has paved the avenue for developing new prophylactic and therapeutic agents with broad-spectrum antiviral activities.

Electronic supplementary material

The online version of this article (doi:10.1038/srep22008) contains supplementary material, which is available to authorized users.


Url:
DOI: 10.1038/srep22008
PubMed: 26911565
PubMed Central: 4766503


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<name sortKey="Zheng, Bo Jian" sort="Zheng, Bo Jian" uniqKey="Zheng B" first="Bo-Jian" last="Zheng">Bo-Jian Zheng</name>
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<institution-id institution-id-type="GRID">grid.194645.b</institution-id>
<institution-id institution-id-type="ISNI">0000000121742757</institution-id>
<institution>Department of Microbiology,</institution>
<institution>The University of Hong Kong,</institution>
</institution-wrap>
Hong Kong, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
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</author>
</analytic>
<series>
<title level="j">Scientific Reports</title>
<idno type="eISSN">2045-2322</idno>
<imprint>
<date when="2016">2016</date>
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<term>Animals</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Endosomes (drug effects)</term>
<term>Endosomes (metabolism)</term>
<term>Endosomes (virology)</term>
<term>Influenza A virus (drug effects)</term>
<term>Influenza A virus (physiology)</term>
<term>Inhibitory Concentration 50</term>
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<term>Endosomes (métabolisme)</term>
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<term>Fragments peptidiques (pharmacologie)</term>
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<term>Infections à Orthomyxoviridae (virologie)</term>
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<term>Middle East Respiratory Syndrome Coronavirus</term>
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<term>Orthomyxoviridae Infections</term>
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<front>
<div type="abstract" xml:lang="en">
<p>A safe, potent and broad-spectrum antiviral is urgently needed to combat emerging respiratory viruses. In light of the broad antiviral activity of β-defensins, we tested the antiviral activity of 11 peptides derived from mouse β-defensin-4 and found that a short peptide, P9, exhibited potent and broad-spectrum antiviral effects against multiple respiratory viruses
<italic>in vitro</italic>
and
<italic>in vivo</italic>
, including influenza A virus H1N1, H3N2, H5N1, H7N7, H7N9, SARS-CoV and MERS-CoV. The antiviral activity of P9 was attributed to its high-affinity binding to viral glycoproteins, as well as the abundance of basic amino acids in its composition. After binding viral particles through viral surface glycoproteins, P9 entered into cells together with the viruses via endocytosis and prevented endosomal acidification, which blocked membrane fusion and subsequent viral RNA release. This study has paved the avenue for developing new prophylactic and therapeutic agents with broad-spectrum antiviral activities.</p>
<sec>
<title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1038/srep22008) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
</front>
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