The antiviral activity of poly-γ-glutamic acid, a polypeptide secreted by Bacillus sp., through induction of CD14-dependent type I interferon responses.
Identifieur interne : 001130 ( PubMed/Corpus ); précédent : 001129; suivant : 001131The antiviral activity of poly-γ-glutamic acid, a polypeptide secreted by Bacillus sp., through induction of CD14-dependent type I interferon responses.
Auteurs : Wooseong Lee ; Seung-Hoon Lee ; Dae-Gyun Ahn ; Hee Cho ; Moon-Hee Sung ; Seung Hyun Han ; Jong-Won OhSource :
- Biomaterials [ 1878-5905 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (metabolism), Antiviral Agents (therapeutic use), Bacillus (metabolism), Cell Line, HEK293 Cells, Hepacivirus (drug effects), Hepatitis C (drug therapy), Humans, Interferon Type I (immunology), Lipopolysaccharide Receptors (immunology), Mice, Polyglutamic Acid (analogs & derivatives), Polyglutamic Acid (metabolism), Polyglutamic Acid (therapeutic use), SARS Virus (drug effects), Severe Acute Respiratory Syndrome (drug therapy), Toll-Like Receptor 4 (immunology).
- MESH :
- chemical , analogs & derivatives : Polyglutamic Acid.
- chemical , immunology : Interferon Type I, Lipopolysaccharide Receptors, Toll-Like Receptor 4.
- chemical , metabolism : Antiviral Agents, Polyglutamic Acid.
- chemical , therapeutic use : Antiviral Agents, Polyglutamic Acid.
- drug effects : Hepacivirus, SARS Virus.
- drug therapy : Hepatitis C, Severe Acute Respiratory Syndrome.
- metabolism : Bacillus.
- Animals, Cell Line, HEK293 Cells, Humans, Mice.
Abstract
Poly-γ-glutamic acid (γ-PGA) is an anionic polypeptide secreted by Bacillus sp. that has been shown to activate immune cells through interactions with toll-like receptor 4 (TLR4). However, its ability to induce the type I interferon (IFN) response has not yet been characterized. Here, we demonstrate that γ-PGA induces type I IFN signaling pathway via the TLR4 signaling pathway. The induction required both myeloid differentiation factor 2 (MD2) and the pattern-recognition receptor CD14, which are two TLR4-associated accessory proteins. The γ-PGA with high molecular weights (2000 and 5000 kDa) was able to activate the subsequent signals through TLR4/MD2 to result in dimerization of IRF-3, a transcription factor required for IFN gene expression, leading to increases in mRNA levels of the type I IFN-response genes, 2'-5' OAS and ISG56. Moreover, γ-PGA (2000 kDa) displayed an antiviral activity against SARS coronavirus and hepatitis C virus. Our results identify high-molecular weight γ-PGA as a TLR4 ligand and demonstrate that γ-PGA requires both CD14 and MD2 for the activation of type I IFN responses. Our results suggest that the microbial biopolymer γ-PGA may have therapeutic potential against a broad range of viruses sensitive to type I IFNs.
DOI: 10.1016/j.biomaterials.2013.08.067
PubMed: 24016850
Links to Exploration step
pubmed:24016850Le document en format XML
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Moon Hee" uniqKey="Sung M" first="Moon-Hee" last="Sung">Moon-Hee Sung</name></author><author><name sortKey="Han, Seung Hyun" sort="Han, Seung Hyun" uniqKey="Han S" first="Seung Hyun" last="Han">Seung Hyun Han</name></author><author><name sortKey="Oh, Jong Won" sort="Oh, Jong Won" uniqKey="Oh J" first="Jong-Won" last="Oh">Jong-Won Oh</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:24016850</idno><idno type="pmid">24016850</idno><idno type="doi">10.1016/j.biomaterials.2013.08.067</idno><idno type="wicri:Area/PubMed/Corpus">001130</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001130</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The antiviral activity of poly-γ-glutamic acid, a polypeptide secreted by Bacillus sp., through induction of CD14-dependent type I interferon responses.</title><author><name sortKey="Lee, Wooseong" sort="Lee, Wooseong" uniqKey="Lee W" first="Wooseong" last="Lee">Wooseong Lee</name><affiliation><nlm:affiliation>Department of Biotechnology and Center for Protein Function Control, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 120-749, Republic of Korea.</nlm:affiliation></affiliation></author><author><name sortKey="Lee, Seung Hoon" sort="Lee, Seung Hoon" uniqKey="Lee S" first="Seung-Hoon" last="Lee">Seung-Hoon Lee</name></author><author><name sortKey="Ahn, Dae Gyun" sort="Ahn, Dae Gyun" uniqKey="Ahn D" first="Dae-Gyun" last="Ahn">Dae-Gyun Ahn</name></author><author><name sortKey="Cho, Hee" sort="Cho, Hee" uniqKey="Cho H" first="Hee" last="Cho">Hee Cho</name></author><author><name sortKey="Sung, Moon Hee" sort="Sung, Moon Hee" uniqKey="Sung M" first="Moon-Hee" last="Sung">Moon-Hee Sung</name></author><author><name sortKey="Han, Seung Hyun" sort="Han, Seung Hyun" uniqKey="Han S" first="Seung Hyun" last="Han">Seung Hyun Han</name></author><author><name sortKey="Oh, Jong Won" sort="Oh, Jong Won" uniqKey="Oh J" first="Jong-Won" last="Oh">Jong-Won Oh</name></author></analytic><series><title level="j">Biomaterials</title><idno type="eISSN">1878-5905</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antiviral Agents (metabolism)</term><term>Antiviral Agents (therapeutic use)</term><term>Bacillus (metabolism)</term><term>Cell Line</term><term>HEK293 Cells</term><term>Hepacivirus (drug effects)</term><term>Hepatitis C (drug therapy)</term><term>Humans</term><term>Interferon Type I (immunology)</term><term>Lipopolysaccharide Receptors (immunology)</term><term>Mice</term><term>Polyglutamic Acid (analogs & derivatives)</term><term>Polyglutamic Acid (metabolism)</term><term>Polyglutamic Acid (therapeutic use)</term><term>SARS Virus (drug effects)</term><term>Severe Acute Respiratory Syndrome (drug therapy)</term><term>Toll-Like Receptor 4 (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Interferon Type I</term><term>Lipopolysaccharide Receptors</term><term>Toll-Like Receptor 4</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antiviral Agents</term><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Antiviral Agents</term><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Hepacivirus</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Hepatitis C</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Poly-γ-glutamic acid (γ-PGA) is an anionic polypeptide secreted by Bacillus sp. that has been shown to activate immune cells through interactions with toll-like receptor 4 (TLR4). However, its ability to induce the type I interferon (IFN) response has not yet been characterized. Here, we demonstrate that γ-PGA induces type I IFN signaling pathway via the TLR4 signaling pathway. The induction required both myeloid differentiation factor 2 (MD2) and the pattern-recognition receptor CD14, which are two TLR4-associated accessory proteins. The γ-PGA with high molecular weights (2000 and 5000 kDa) was able to activate the subsequent signals through TLR4/MD2 to result in dimerization of IRF-3, a transcription factor required for IFN gene expression, leading to increases in mRNA levels of the type I IFN-response genes, 2'-5' OAS and ISG56. Moreover, γ-PGA (2000 kDa) displayed an antiviral activity against SARS coronavirus and hepatitis C virus. Our results identify high-molecular weight γ-PGA as a TLR4 ligand and demonstrate that γ-PGA requires both CD14 and MD2 for the activation of type I IFN responses. Our results suggest that the microbial biopolymer γ-PGA may have therapeutic potential against a broad range of viruses sensitive to type I IFNs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24016850</PMID><DateCompleted><Year>2014</Year><Month>04</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-5905</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>37</Issue><PubDate><Year>2013</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biomaterials</Title><ISOAbbreviation>Biomaterials</ISOAbbreviation></Journal><ArticleTitle>The antiviral activity of poly-γ-glutamic acid, a polypeptide secreted by Bacillus sp., through induction of CD14-dependent type I interferon responses.</ArticleTitle><Pagination><MedlinePgn>9700-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.biomaterials.2013.08.067</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0142-9612(13)01030-2</ELocationID><Abstract><AbstractText>Poly-γ-glutamic acid (γ-PGA) is an anionic polypeptide secreted by Bacillus sp. that has been shown to activate immune cells through interactions with toll-like receptor 4 (TLR4). However, its ability to induce the type I interferon (IFN) response has not yet been characterized. Here, we demonstrate that γ-PGA induces type I IFN signaling pathway via the TLR4 signaling pathway. The induction required both myeloid differentiation factor 2 (MD2) and the pattern-recognition receptor CD14, which are two TLR4-associated accessory proteins. The γ-PGA with high molecular weights (2000 and 5000 kDa) was able to activate the subsequent signals through TLR4/MD2 to result in dimerization of IRF-3, a transcription factor required for IFN gene expression, leading to increases in mRNA levels of the type I IFN-response genes, 2'-5' OAS and ISG56. Moreover, γ-PGA (2000 kDa) displayed an antiviral activity against SARS coronavirus and hepatitis C virus. Our results identify high-molecular weight γ-PGA as a TLR4 ligand and demonstrate that γ-PGA requires both CD14 and MD2 for the activation of type I IFN responses. Our results suggest that the microbial biopolymer γ-PGA may have therapeutic potential against a broad range of viruses sensitive to type I IFNs.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Wooseong</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Center for Protein Function Control, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 120-749, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Seung-Hoon</ForeName><Initials>SH</Initials></Author><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>Dae-Gyun</ForeName><Initials>DG</Initials></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Hee</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Sung</LastName><ForeName>Moon-Hee</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Han</LastName><ForeName>Seung Hyun</ForeName><Initials>SH</Initials></Author><Author 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