Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus
Identifieur interne : 000813 ( Istex/Corpus ); précédent : 000812; suivant : 000814Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus
Auteurs : G. S. Sidhu ; A. K. Singh ; P. N. Raghunath ; S. Sivaram ; R. K. MaheshwariSource :
- Virus Research [ 0168-1702 ] ; 1996.
English descriptors
- Teeft :
- Antiviral, Antiviral action, Antiviral activity, Assay, Biol, Brefeldin, Cellular extracts, Dependent rnase, Dos, Emcv, Endoplasmic reticulum, Housekeeping gene, Hovanessian, Hybridization, Interferon, Internal control, Intracellular transport, Kinase, Lysis buffer, Northern hybridization, Nuclease, Phosphorylation, Poly, Present study, Primer, Protein kinase, Protein synthesis, Replication, Rnase, Secretory proteins, Sidhu, Silverman, Supernatant, Synthetase, Uninfected, Uninfected cells, Untreated control cells, Various concentrations, Various doses, Virol, Virus research.
Abstract
Abstract: Brefeldin A (BFA), a unique fungal metabolite of a 13-membered lactone ring, exhibits various biological actions, including antitumor, antifungal and antiviral activities. In the present study, mouse LB cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in LB cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.
Url:
DOI: 10.1016/0168-1702(95)01262-1
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ISTEX:BE70009D7214285719A57EFEDE9129B09B3DABA4Le document en format XML
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Sidhu</name><affiliation><mods:affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</mods:affiliation></affiliation></author><author><name sortKey="Singh, A K" sort="Singh, A K" uniqKey="Singh A" first="A. K." last="Singh">A. K. Singh</name><affiliation><mods:affiliation>Birla Institute of Technology and Science, Pilani Rajasthan, India</mods:affiliation></affiliation></author><author><name sortKey="Raghunath, P N" sort="Raghunath, P N" uniqKey="Raghunath P" first="P. N." last="Raghunath">P. N. Raghunath</name><affiliation><mods:affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</mods:affiliation></affiliation></author><author><name sortKey="Sivaram, S" sort="Sivaram, S" uniqKey="Sivaram S" first="S." last="Sivaram">S. Sivaram</name><affiliation><mods:affiliation>Birla Institute of Technology and Science, Pilani Rajasthan, India</mods:affiliation></affiliation></author><author><name sortKey="Maheshwari, R K" sort="Maheshwari, R K" uniqKey="Maheshwari R" first="R. K." last="Maheshwari">R. K. Maheshwari</name><affiliation><mods:affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Virus Research</title><title level="j" type="abbrev">VIRUS</title><idno type="ISSN">0168-1702</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">40</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="123">123</biblScope><biblScope unit="page" to="133">133</biblScope></imprint><idno type="ISSN">0168-1702</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0168-1702</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Antiviral</term><term>Antiviral action</term><term>Antiviral activity</term><term>Assay</term><term>Biol</term><term>Brefeldin</term><term>Cellular extracts</term><term>Dependent rnase</term><term>Dos</term><term>Emcv</term><term>Endoplasmic reticulum</term><term>Housekeeping gene</term><term>Hovanessian</term><term>Hybridization</term><term>Interferon</term><term>Internal control</term><term>Intracellular transport</term><term>Kinase</term><term>Lysis buffer</term><term>Northern hybridization</term><term>Nuclease</term><term>Phosphorylation</term><term>Poly</term><term>Present study</term><term>Primer</term><term>Protein kinase</term><term>Protein synthesis</term><term>Replication</term><term>Rnase</term><term>Secretory proteins</term><term>Sidhu</term><term>Silverman</term><term>Supernatant</term><term>Synthetase</term><term>Uninfected</term><term>Uninfected cells</term><term>Untreated control cells</term><term>Various concentrations</term><term>Various doses</term><term>Virol</term><term>Virus research</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Brefeldin A (BFA), a unique fungal metabolite of a 13-membered lactone ring, exhibits various biological actions, including antitumor, antifungal and antiviral activities. In the present study, mouse LB cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in LB cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>synthetase</json:string><json:string>emcv</json:string><json:string>antiviral</json:string><json:string>interferon</json:string><json:string>brefeldin</json:string><json:string>rnase</json:string><json:string>poly</json:string><json:string>hybridization</json:string><json:string>antiviral activity</json:string><json:string>uninfected</json:string><json:string>nuclease</json:string><json:string>kinase</json:string><json:string>dependent rnase</json:string><json:string>hovanessian</json:string><json:string>virus research</json:string><json:string>phosphorylation</json:string><json:string>sidhu</json:string><json:string>cellular extracts</json:string><json:string>biol</json:string><json:string>virol</json:string><json:string>protein kinase</json:string><json:string>primer</json:string><json:string>silverman</json:string><json:string>lysis buffer</json:string><json:string>assay</json:string><json:string>dos</json:string><json:string>replication</json:string><json:string>antiviral action</json:string><json:string>present study</json:string><json:string>internal control</json:string><json:string>protein synthesis</json:string><json:string>uninfected cells</json:string><json:string>supernatant</json:string><json:string>northern hybridization</json:string><json:string>untreated control cells</json:string><json:string>various concentrations</json:string><json:string>endoplasmic reticulum</json:string><json:string>housekeeping gene</json:string><json:string>various doses</json:string><json:string>secretory proteins</json:string><json:string>intracellular transport</json:string></teeft></keywords><author><json:item><name>G.S. Sidhu</name><affiliations><json:string>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</json:string></affiliations></json:item><json:item><name>A.K. Singh</name><affiliations><json:string>Birla Institute of Technology and Science, Pilani Rajasthan, India</json:string></affiliations></json:item><json:item><name>P.N. Raghunath</name><affiliations><json:string>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</json:string></affiliations></json:item><json:item><name>S. Sivaram</name><affiliations><json:string>Birla Institute of Technology and Science, Pilani Rajasthan, India</json:string></affiliations></json:item><json:item><name>R.K. Maheshwari</name><affiliations><json:string>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Brefeldin A</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MouseLB cells</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Interferon</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Encephalomyocarditis</value></json:item></subject><arkIstex>ark:/67375/6H6-KM11Q7F2-L</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Brefeldin A (BFA), a unique fungal metabolite of a 13-membered lactone ring, exhibits various biological actions, including antitumor, antifungal and antiviral activities. In the present study, mouse LB cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in LB cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.</abstract><qualityIndicators><score>9.58</score><pdfWordCount>5443</pdfWordCount><pdfCharCount>31919</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>540 x 764 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>215</abstractWordCount><abstractCharCount>1479</abstractCharCount><keywordCount>4</keywordCount></qualityIndicators><title>Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus</title><pmid><json:string>8725108</json:string></pmid><pii><json:string>0168-1702(95)01262-1</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. 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Sidhu et al.</json:string><json:string>Fujiwara et al., 1988</json:string><json:string>Misumi et al., 1986</json:string><json:string>Stark et al., 1982</json:string><json:string>Singh et al., 1988</json:string><json:string>Farrell et al., 1977</json:string><json:string>Lippincott-Schwartz et al., 1989</json:string><json:string>Levintow, 1974</json:string><json:string>Nolan-Sorden et al., 1990</json:string><json:string>Samuel, 1988</json:string><json:string>Reaves and Banting, 1992</json:string><json:string>Takatsuki and Tamura, 1985</json:string><json:string>Hovanessian, 1989</json:string><json:string>Kerr et al., 1974</json:string><json:string>Gupta et al., 1982</json:string><json:string>Galabru and Hovanessian, 1987</json:string><json:string>Tamura et al., 1968</json:string><json:string>Williams et al., 1979</json:string><json:string>Safer, 1983</json:string><json:string>Hovanessian et al., 1987</json:string><json:string>Chen et al., 1991</json:string><json:string>Knight et al., 1980</json:string><json:string>Pestka et al., 1987</json:string><json:string>Whealy et al., 1991</json:string><json:string>Silverman et al., 1982</json:string><json:string>Maniatis et al., 1982</json:string><json:string>Doms et al., 1989</json:string><json:string>Maynell et al., 1992</json:string><json:string>Cheung et al., 1991</json:string><json:string>Staeheli, 1990</json:string><json:string>Maheshwari and Friedman, 1979</json:string><json:string>Memet et al., 1991</json:string><json:string>Magner and Papagiannes, 1988</json:string><json:string>Adams and Hamilton, 1988</json:string><json:string>Clemens and Williams, 1978</json:string><json:string>Dubois and Hovanessian, 1990</json:string><json:string>Rice et al., 1985</json:string><json:string>Pal et al., 1991</json:string><json:string>Hovanessian et al., 1979</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-KM11Q7F2-L</json:string></ark><categories><wos><json:string>1 - 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In the present study, mouse LB cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in LB cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Brefeldin A</term></item><item><term>MouseLB cells</term></item><item><term>Interferon</term></item><item><term>Encephalomyocarditis</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995-10-20">Modified</change><change when="1996">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KM11Q7F2-L/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>VIRUS</jid><aid>95012621</aid><ce:pii>0168-1702(95)01262-1</ce:pii><ce:doi>10.1016/0168-1702(95)01262-1</ce:doi><ce:copyright type="unknown" year="1996"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research paper</ce:textfn></ce:dochead><ce:title>Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus</ce:title><ce:author-group><ce:author><ce:given-name>G.S.</ce:given-name><ce:surname>Sidhu</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.K.</ce:given-name><ce:surname>Singh</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>P.N.</ce:given-name><ce:surname>Raghunath</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>S.</ce:given-name><ce:surname>Sivaram</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>R.K.</ce:given-name><ce:surname>Maheshwari</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Birla Institute of Technology and Science, Pilani Rajasthan, India</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="11" month="10" year="1993"></ce:date-received><ce:date-revised day="20" month="10" year="1995"></ce:date-revised><ce:date-accepted day="20" month="10" year="1995"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Brefeldin A (BFA), a unique fungal metabolite of a 13-membered lactone ring, exhibits various biological actions, including antitumor, antifungal and antiviral activities. In the present study, mouse L<ce:inf>B</ce:inf> cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in L<ce:inf>B</ce:inf> cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Brefeldin A</ce:text></ce:keyword><ce:keyword><ce:text>MouseL<ce:inf>B</ce:inf> cells</ce:text></ce:keyword><ce:keyword><ce:text>Interferon</ce:text></ce:keyword><ce:keyword><ce:text>Encephalomyocarditis</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Brefeldin A inhibits the antiviral action of interferon against encephalomyocarditis virus</title></titleInfo><name type="personal"><namePart type="given">G.S.</namePart><namePart type="family">Sidhu</namePart><affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</affiliation><description>Corresponding author.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.K.</namePart><namePart type="family">Singh</namePart><affiliation>Birla Institute of Technology and Science, Pilani Rajasthan, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.N.</namePart><namePart type="family">Raghunath</namePart><affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Sivaram</namePart><affiliation>Birla Institute of Technology and Science, Pilani Rajasthan, India</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.K.</namePart><namePart type="family">Maheshwari</namePart><affiliation>Department of Pathology, Uniformed Services University of Health Sciences, Bethesda, MD 20814-4799, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued><dateModified encoding="w3cdtf">1995-10-20</dateModified><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Brefeldin A (BFA), a unique fungal metabolite of a 13-membered lactone ring, exhibits various biological actions, including antitumor, antifungal and antiviral activities. In the present study, mouse LB cells were treated with various concentrations of interferon (IFN) and/or BFA overnight and infected with encephalomyocarditis virus (EMCV) after removal of IFN and BFA. Doses of BFA which neither inhibit the metabolism of the cell nor the infectivity of EMCV, decreased the IFN-induced antiviral activity against EMCV as demonstrated by virus titer from supernatants. Since 2–5A synthetase and double-stranded RNA (dsRNA)-dependent protein kinase (PKR) have been suggested to be involved in the antiviral action of IFN against EMCV, their activities were investigated in LB cells after BFA treatment. Northern blot analysis and in situ hybridization showed a decrease (2–3-fold) in the mRNA of 2′–5′ oligoadenylate (2–5A) synthetase after BFA treatment. BFA also inhibited the activity of 2–5A synthetase, 2–5A dependent RNase and phosphorylation of PKR in cellular extracts, indicating that BFA may be exerting its inhibitory effect both at the transcriptional and post-transcriptional levels. This study reports a new biological action of BFA, demonstrating that BFA antagonized the antiviral action of IFN by inhibiting IFN-induced enzymatic pathways. These studies also suggest that both 2–5A and PKR are important in the antiviral activity of IFN against EMCV.</abstract><note type="content">Section title: Research paper</note><subject><genre>Keywords</genre><topic>Brefeldin A</topic><topic>MouseLB cells</topic><topic>Interferon</topic><topic>Encephalomyocarditis</topic></subject><relatedItem type="host"><titleInfo><title>Virus Research</title></titleInfo><titleInfo type="abbreviated"><title>VIRUS</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued></originInfo><identifier type="ISSN">0168-1702</identifier><identifier type="PII">S0168-1702(00)X0003-2</identifier><part><date>1996</date><detail type="volume"><number>40</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>113</start><end>211</end></extent><extent unit="pages"><start>123</start><end>133</end></extent></part></relatedItem><identifier type="istex">BE70009D7214285719A57EFEDE9129B09B3DABA4</identifier><identifier type="ark">ark:/67375/6H6-KM11Q7F2-L</identifier><identifier type="DOI">10.1016/0168-1702(95)01262-1</identifier><identifier type="PII">0168-1702(95)01262-1</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KM11Q7F2-L/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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