Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid
Identifieur interne : 001076 ( Istex/Corpus ); précédent : 001075; suivant : 001077Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid
Auteurs : P. Meindl ; G. Bodo ; P. Palese ; J. Schulman ; H. TuppySource :
- Virology [ 0042-6822 ] ; 1974.
English descriptors
- Teeft :
- Academic press, Acid, Amino group, Bacterial sources, Carbon atom, Cell receptors, Cholerae, Cholerae neuraminidase, Derivative, Different compounds, Different substitutions, Enzyme inhibition, Fetuin, Hemagglutination, Hemagglutination inhibition, Hon2, Influenza, Influenza virus, Influenza virus neuraminidase, Inhibition, Inhibitor, Inhibitor concentration, Inhibitory activity, Meindl, Methyl esters, Myxovirus, Nacetylneuraminic acid, Neuraminic, Neuraminic acid analogs, Neuraminic acid derivatives, Neuraminidase, Neuraminidase activity, Neuraminidase inhibition, Neuraminidase inhibitors, Neuraminidases, Newcastle disease virus, Palese, Parainfluenza virus type, Parainfluenza viruses, Phosphate buffer, Potent neuraminidase inhibitor, Reaction mixture, Sendai virus, Standard procedures, Synthetic inhibitors, Tissue culture, Tuppy, Unpublished results, Vibrio cholerae neuraminidase, Viral, Viral neuraminidases, Weight substrate.
Abstract
Abstract: Eighteen derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid were assayed for inhibitory activity against neuraminidases from viral and bacterial sources. Twelve of these compounds were active against neuraminidases of Vibrio cholerae, influenza AMel, BLee, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10−3M to 10−6M. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (Ki) of 7,9 × 10−7, M for influenza AMel virus neuraminidase whereas the Km of the virus enzyme for the substrate is 1000 times weaker (Km = 6, 9 × 10−4M). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.
Url:
DOI: 10.1016/0042-6822(74)90080-4
Links to Exploration step
ISTEX:8FFBE048372A94739993860AB41F5521DB27C3CDLe document en format XML
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Twelve of these compounds were active against neuraminidases of Vibrio cholerae, influenza AMel, BLee, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10−3M to 10−6M. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (Ki) of 7,9 × 10−7, M for influenza AMel virus neuraminidase whereas the Km of the virus enzyme for the substrate is 1000 times weaker (Km = 6, 9 × 10−4M). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>neuraminidases</json:string><json:string>neuraminic</json:string><json:string>meindl</json:string><json:string>hemagglutination</json:string><json:string>tuppy</json:string><json:string>viral</json:string><json:string>cholerae</json:string><json:string>hon2</json:string><json:string>palese</json:string><json:string>myxovirus</json:string><json:string>fetuin</json:string><json:string>inhibitor</json:string><json:string>influenza</json:string><json:string>influenza virus</json:string><json:string>derivative</json:string><json:string>neuraminidase activity</json:string><json:string>inhibitory activity</json:string><json:string>reaction mixture</json:string><json:string>neuraminidase inhibition</json:string><json:string>sendai virus</json:string><json:string>viral neuraminidases</json:string><json:string>enzyme inhibition</json:string><json:string>amino group</json:string><json:string>parainfluenza viruses</json:string><json:string>newcastle disease virus</json:string><json:string>nacetylneuraminic acid</json:string><json:string>tissue culture</json:string><json:string>cholerae neuraminidase</json:string><json:string>acid</json:string><json:string>inhibition</json:string><json:string>phosphate buffer</json:string><json:string>different substitutions</json:string><json:string>unpublished results</json:string><json:string>methyl esters</json:string><json:string>standard procedures</json:string><json:string>parainfluenza virus type</json:string><json:string>carbon atom</json:string><json:string>weight substrate</json:string><json:string>neuraminidase inhibitors</json:string><json:string>academic press</json:string><json:string>neuraminic acid derivatives</json:string><json:string>synthetic inhibitors</json:string><json:string>influenza virus neuraminidase</json:string><json:string>inhibitor concentration</json:string><json:string>neuraminic acid analogs</json:string><json:string>potent neuraminidase inhibitor</json:string><json:string>different compounds</json:string><json:string>bacterial sources</json:string><json:string>hemagglutination inhibition</json:string><json:string>cell receptors</json:string><json:string>vibrio cholerae neuraminidase</json:string></teeft></keywords><author><json:item><name>P. Meindl</name><affiliations><json:string>Arzneimittelforschung GmbH, Vienna A-1121, Austria</json:string></affiliations></json:item><json:item><name>G. Bodo</name><affiliations><json:string>Arzneimittelforschung GmbH, Vienna A-1121, Austria</json:string></affiliations></json:item><json:item><name>P. Palese</name><affiliations><json:string>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</json:string></affiliations></json:item><json:item><name>J. Schulman</name><affiliations><json:string>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</json:string></affiliations></json:item><json:item><name>H. Tuppy</name><affiliations><json:string>Institut für Biochemie, University of Vienna, Vienna, Austria</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-RVXNGXDC-V</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Eighteen derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid were assayed for inhibitory activity against neuraminidases from viral and bacterial sources. Twelve of these compounds were active against neuraminidases of Vibrio cholerae, influenza AMel, BLee, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10−3M to 10−6M. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (Ki) of 7,9 × 10−7, M for influenza AMel virus neuraminidase whereas the Km of the virus enzyme for the substrate is 1000 times weaker (Km = 6, 9 × 10−4M). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>140</abstractWordCount><abstractCharCount>1012</abstractCharCount><keywordCount>0</keywordCount><score>6.03</score><pdfWordCount>2350</pdfWordCount><pdfCharCount>20623</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize></qualityIndicators><title>Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid</title><pmid><json:string>4362431</json:string></pmid><pii><json:string>0042-6822(74)90080-4</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Perspectives in Virology</title><language><json:string>unknown</json:string></language><volume>Vol. 5</volume><pages><first>87</first><last>106</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1974</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0346-7</json:string></pii><volume>58</volume><issue>2</issue><pages><first>457</first><last>463</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1974</json:string><json:string>1000</json:string></date><geogName></geogName><orgName><json:string>Army Medical Research and Development Command</json:string><json:string>Health Research Council of the City of New York</json:string><json:string>Austria Accepted December Sinai</json:string><json:string>Commission on Influenza of the Armed Forces Epidemiological Board</json:string><json:string>University of Vienna</json:string><json:string>National Institute of Allergy and Infectious Diseases</json:string><json:string>Academic Press, Inc.</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Ursula Schlosser</json:string><json:string>Peter Lima</json:string></persName><placeName><json:string>Germany</json:string><json:string>Austria</json:string><json:string>Sendai</json:string><json:string>Melbourne</json:string><json:string>Vienna</json:string><json:string>York</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Meindl and Tuppy, 1967</json:string><json:string>Sever, 1962</json:string><json:string>Meindl and Tuppy, 196913</json:string><json:string>Scheid et al., 1972</json:string><json:string>Kilbourne et al., 1967</json:string><json:string>Scheid and Choppin, 1973</json:string><json:string>Meindl and Tuppy, 1969a</json:string><json:string>Haskell et al., 1970</json:string><json:string>Meindl et al., 1971</json:string><json:string>Edmond et al., 1966</json:string><json:string>Palese et al.</json:string><json:string>Palese and Schulman, 1974</json:string><json:string>Tuppy (196910)</json:string><json:string>Becht and Drzeniek, 1967</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-RVXNGXDC-V</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string><json:string>4 - nephrologie. maladies des voies urinaires</json:string></inist></categories><publicationDate>1974</publicationDate><copyrightDate>1974</copyrightDate><doi><json:string>10.1016/0042-6822(74)90080-4</json:string></doi><id>8FFBE048372A94739993860AB41F5521DB27C3CD</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-RVXNGXDC-V/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-RVXNGXDC-V/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-RVXNGXDC-V/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1974</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid</title><author xml:id="author-0000"><persName><forename type="first">P.</forename><surname>Meindl</surname></persName><affiliation>Arzneimittelforschung GmbH, Vienna A-1121, Austria</affiliation></author><author xml:id="author-0001"><persName><forename type="first">G.</forename><surname>Bodo</surname></persName><affiliation>Arzneimittelforschung GmbH, Vienna A-1121, Austria</affiliation></author><author xml:id="author-0002"><persName><forename type="first">P.</forename><surname>Palese</surname></persName><affiliation>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">J.</forename><surname>Schulman</surname></persName><affiliation>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</affiliation></author><author xml:id="author-0004"><persName><forename type="first">H.</forename><surname>Tuppy</surname></persName><affiliation>Institut für Biochemie, University of Vienna, Vienna, Austria</affiliation></author><idno type="istex">8FFBE048372A94739993860AB41F5521DB27C3CD</idno><idno type="ark">ark:/67375/6H6-RVXNGXDC-V</idno><idno type="DOI">10.1016/0042-6822(74)90080-4</idno><idno type="PII">0042-6822(74)90080-4</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0346-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1974"></date><biblScope unit="volume">58</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="457">457</biblScope><biblScope unit="page" to="463">463</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1974</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Eighteen derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid were assayed for inhibitory activity against neuraminidases from viral and bacterial sources. Twelve of these compounds were active against neuraminidases of Vibrio cholerae, influenza AMel, BLee, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10−3M to 10−6M. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (Ki) of 7,9 × 10−7, M for influenza AMel virus neuraminidase whereas the Km of the virus enzyme for the substrate is 1000 times weaker (Km = 6, 9 × 10−4M). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.</p></abstract></profileDesc><revisionDesc><change when="1974">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-RVXNGXDC-V/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>YVIRO</jid><aid>74900804</aid><ce:pii>0042-6822(74)90080-4</ce:pii><ce:doi>10.1016/0042-6822(74)90080-4</ce:doi><ce:copyright type="unknown" year="1974"></ce:copyright></item-info><head><ce:title>Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-<ce:italic>N</ce:italic>-acetylneuraminic acid</ce:title><ce:author-group><ce:author><ce:given-name>P.</ce:given-name><ce:surname>Meindl</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Bodo</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>P.</ce:given-name><ce:surname>Palese</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.</ce:given-name><ce:surname>Schulman</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>H.</ce:given-name><ce:surname>Tuppy</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Arzneimittelforschung GmbH, Vienna A-1121, Austria</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Institut für Biochemie, University of Vienna, Vienna, Austria</ce:textfn></ce:affiliation></ce:author-group><ce:date-accepted day="10" month="12" year="1973"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Eighteen derivatives of 2-deoxy-2,3-dehydro-<ce:italic>N</ce:italic>-acetylneuraminic acid were assayed for inhibitory activity against neuraminidases from viral and bacterial sources. Twelve of these compounds were active against neuraminidases of <ce:italic>Vibrio cholerae</ce:italic>, influenza <math altimg="si1.gif"><fr shape="sol"><nu><rm>A</rm></nu><de><rm>Mel</rm></de></fr>, <fr shape="sol"><nu><rm>B</rm></nu><de><rm>Lee</rm></de></fr></math>, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10<ce:sup>−3</ce:sup><ce:italic>M</ce:italic> to 10<ce:sup>−6</ce:sup><ce:italic>M</ce:italic>. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-<ce:italic>N</ce:italic>-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (<ce:italic>K</ce:italic><ce:inf><ce:italic>i</ce:italic></ce:inf>) of 7,9 × 10<ce:sup>−7</ce:sup>, <ce:italic>M</ce:italic> for influenza <math altimg="si2.gif"><fr shape="sol"><nu><rm>A</rm></nu><de><rm>Mel</rm></de></fr></math> virus neuraminidase whereas the <ce:italic>K</ce:italic><ce:inf><ce:italic>m</ce:italic></ce:inf> of the virus enzyme for the substrate is 1000 times weaker (<ce:italic>K</ce:italic><ce:inf><ce:italic>m</ce:italic></ce:inf> = 6, 9 × 10<ce:sup>−4</ce:sup><ce:italic>M</ce:italic>). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-<ce:italic>N</ce:italic>-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro- N -acetylneuraminic acid</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-</title></titleInfo><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Meindl</namePart><affiliation>Arzneimittelforschung GmbH, Vienna A-1121, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Bodo</namePart><affiliation>Arzneimittelforschung GmbH, Vienna A-1121, Austria</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Palese</namePart><affiliation>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">Schulman</namePart><affiliation>Department of Microbiology, Mt. Sinai School of Medicine of CUNY, New York, New York 10089 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Tuppy</namePart><affiliation>Institut für Biochemie, University of Vienna, Vienna, Austria</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">1974</dateIssued><copyrightDate encoding="w3cdtf">1974</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Eighteen derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid were assayed for inhibitory activity against neuraminidases from viral and bacterial sources. Twelve of these compounds were active against neuraminidases of Vibrio cholerae, influenza AMel, BLee, and Newcastle disease virus, causing 50% enzyme inhibition in concentrations ranging from 10−3M to 10−6M. The most active of them and the most potent neuraminidase inhibitor described so far is 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid. This compound has an inhibitor constant (Ki) of 7,9 × 10−7, M for influenza AMel virus neuraminidase whereas the Km of the virus enzyme for the substrate is 1000 times weaker (Km = 6, 9 × 10−4M). The mechanism of inhibition is competitive, and enzyme inhibition is independent of enzyme concentration. 2-Deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid inhibits hemagglutination by NDV and SV5 but does not inhibit agglutination of red cells by Sendai virus or influenza A and B viruses.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</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">1974</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0346-7</identifier><part><date>1974</date><detail type="volume"><number>58</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>317</start><end>615</end></extent><extent unit="pages"><start>457</start><end>463</end></extent></part></relatedItem><identifier type="istex">8FFBE048372A94739993860AB41F5521DB27C3CD</identifier><identifier type="ark">ark:/67375/6H6-RVXNGXDC-V</identifier><identifier type="DOI">10.1016/0042-6822(74)90080-4</identifier><identifier type="PII">0042-6822(74)90080-4</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-RVXNGXDC-V/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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