Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display
Identifieur interne : 001974 ( Istex/Corpus ); précédent : 001973; suivant : 001975Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display
Auteurs : J. L. Chagnaud ; D. Moynet ; D. Londos-Gagliardi ; J. H. Bezian ; P. Vincendeau ; H. Fleury ; B. GuillemainSource :
- Letters in Peptide Science [ 0929-5666 ] ; 2001-03-01.
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- KwdEn :
Abstract
Summary: Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies (mAbs). Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. It corresponds to an epitope without direct equivalence with the virus sequence. The data presented here showed that 7G5D8 and DB4 mAbs are raised against linear epitopes while 4F5F6 mAb recognized a continoous topographic epitope.
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DOI: 10.1007/BF02443610
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ISTEX:619B14AF51B66457962728F4F8F2764144E566C0Le document en format XML
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Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. 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Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. It corresponds to an epitope without direct equivalence with the virus sequence. The data presented here showed that 7G5D8 and DB4 mAbs are raised against linear epitopes while 4F5F6 mAb recognized a continoous topographic epitope.</abstract><qualityIndicators><score>9.232</score><pdfWordCount>5901</pdfWordCount><pdfCharCount>34939</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>540 x 738 pts</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>186</abstractWordCount><abstractCharCount>1299</abstractCharCount><keywordCount>6</keywordCount></qualityIndicators><title>Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</title><genre><json:string>research-article</json:string></genre><host><title>Letters in Peptide Science</title><language><json:string>unknown</json:string></language><publicationDate>2001</publicationDate><copyrightDate>2002</copyrightDate><issn><json:string>0929-5666</json:string></issn><eissn><json:string>1573-496X</json:string></eissn><journalId><json:string>10989</json:string></journalId><volume>8</volume><issue>2</issue><pages><first>95</first><last>106</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Polymer Sciences</value></json:item><json:item><value>Biochemistry, general</value></json:item><json:item><value>Animal Anatomy / Morphology / Histology</value></json:item></subject></host><ark><json:string>ark:/67375/VQC-Z2JLQ57G-8</json:string></ark><publicationDate>2001</publicationDate><copyrightDate>2002</copyrightDate><doi><json:string>10.1007/BF02443610</json:string></doi><id>619B14AF51B66457962728F4F8F2764144E566C0</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Z2JLQ57G-8/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Z2JLQ57G-8/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/VQC-Z2JLQ57G-8/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><availability><licence><p>Kluwer Academic Publishers, 2002</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</p></availability><date>2001-07-25</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" type="main" xml:lang="en">Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</title><author xml:id="author-0000"><persName><forename type="first">J.</forename><surname>Chagnaud</surname></persName><affiliation>Laboratoire d'Immunologie Moléculaire et Parasitologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><affiliation>Centre Condorcet 162, GISIR-ADERA, Avenue A. 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Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. It corresponds to an epitope without direct equivalence with the virus sequence. The data presented here showed that 7G5D8 and DB4 mAbs are raised against linear epitopes while 4F5F6 mAb recognized a continoous topographic epitope.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>epitope mapping</term></item><item><term>gp46</term></item><item><term>HTLV-I</term></item><item><term>human retrovirus</term></item><item><term>peptide library</term></item><item><term>phage display</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Polymer Sciences</term></item><item><term>Biochemistry, general</term></item><item><term>Animal Anatomy / Morphology / Histology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2001-07-25">Created</change><change 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NumberingStyle="Unnumbered"><JournalID>10989</JournalID><JournalPrintISSN>0929-5666</JournalPrintISSN><JournalElectronicISSN>1573-496X</JournalElectronicISSN><JournalTitle>Letters in Peptide Science</JournalTitle><JournalAbbreviatedTitle>Lett Pept Sci</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Polymer Sciences</JournalSubject><JournalSubject Type="Secondary">Biochemistry, general</JournalSubject><JournalSubject Type="Secondary">Animal Anatomy / Morphology / Histology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo TocLevels="0" VolumeType="Regular"><VolumeIDStart>8</VolumeIDStart><VolumeIDEnd>8</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd><IssueArticleCount>6</IssueArticleCount><IssueHistory><CoverDate><DateString>2001</DateString><Year>2001</Year><Month>3</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2002</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art5"><ArticleInfo ArticleType="OriginalPaper" ContainsESM="No" Language="En" NumberingStyle="Unnumbered" TocLevels="0"><ArticleID>BF02443610</ArticleID><ArticleDOI>10.1007/BF02443610</ArticleDOI><ArticleSequenceNumber>5</ArticleSequenceNumber><ArticleTitle Language="En">Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</ArticleTitle><ArticleFirstPage>95</ArticleFirstPage><ArticleLastPage>106</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2006</Year><Month>6</Month><Day>8</Day></RegistrationDate><Received><Year>2001</Year><Month>7</Month><Day>25</Day></Received><Revised><Year>2001</Year><Month>11</Month><Day>18</Day></Revised><Accepted><Year>2001</Year><Month>11</Month><Day>18</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2002</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>10989</JournalID><VolumeIDStart>8</VolumeIDStart><VolumeIDEnd>8</VolumeIDEnd><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1 Aff2" PresentAffiliationID="Aff3"><AuthorName DisplayOrder="Western"><GivenName>J.</GivenName><GivenName>L.</GivenName><FamilyName>Chagnaud</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff2" CorrespondingAffiliationID="Aff4"><AuthorName DisplayOrder="Western"><GivenName>D.</GivenName><FamilyName>Moynet</FamilyName></AuthorName><Contact><Fax>(33) 5 57 57 16 52)</Fax><Email>daniel.moynet@immol.u-bordeaux2.fr</Email></Contact></Author><Author AffiliationIDS="Aff5"><AuthorName DisplayOrder="Western"><GivenName>D.</GivenName><FamilyName>Londos-Gagliardi</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff2"><AuthorName DisplayOrder="Western"><GivenName>J.</GivenName><GivenName>H.</GivenName><FamilyName>Bezian</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>P.</GivenName><FamilyName>Vincendeau</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff5"><AuthorName DisplayOrder="Western"><GivenName>H.</GivenName><FamilyName>Fleury</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2 Aff5"><AuthorName DisplayOrder="Western"><GivenName>B.</GivenName><FamilyName>Guillemain</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Laboratoire d'Immunologie Moléculaire et Parasitologie</OrgDivision><OrgName>Université Victor Segalen Bordeaux2</OrgName><OrgAddress><Street>146 rue Léo Saignat</Street><Postcode>33076</Postcode><City>Bordeaux</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Centre Condorcet 162</OrgDivision><OrgName>GISIR-ADERA</OrgName><OrgAddress><Street>Avenue A. Schweitzer BP</Street><Postcode>196 33608</Postcode><City>Pessac</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff5"><OrgDivision>Laboratoire de Virologie</OrgDivision><OrgName>Université Victor Segalen Bordeaux2</OrgName><OrgAddress><Street>146 rue Léo Saignat</Street><Postcode>33076</Postcode><City>Bordeaux</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgName>Diagast Laboratoires</OrgName><OrgAddress><Street>30 Avenue Canteranne</Street><Postcode>33608</Postcode><City>Pessac</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgDivision>Laboratoire d'Immunologie Moléculaire</OrgDivision><OrgName>Université Victor Segalen Bordeaux2</OrgName><OrgAddress><Street>146 rue Léo Saignat</Street><Postcode>33076</Postcode><City>Bordeaux Cedex</City><Country>France</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies (mAbs). Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. It corresponds to an epitope without direct equivalence with the virus sequence. The data presented here showed that 7G5D8 and DB4 mAbs are raised against linear epitopes while 4F5F6 mAb recognized a continoous topographic epitope.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>epitope mapping</Keyword><Keyword>gp46</Keyword><Keyword>HTLV-I</Keyword><Keyword>human retrovirus</Keyword><Keyword>peptide library</Keyword><Keyword>phage display</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Identification of epitopes recognized by monoclonal antibodies directed against HTLV-I envelope surface glycoprotein using peptide phage display</title></titleInfo><name type="personal"><namePart type="given">J.</namePart><namePart type="given">L.</namePart><namePart type="family">Chagnaud</namePart><affiliation>Laboratoire d'Immunologie Moléculaire et Parasitologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><affiliation>Centre Condorcet 162, GISIR-ADERA, Avenue A. Schweitzer BP, 196 33608, Pessac, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">D.</namePart><namePart type="family">Moynet</namePart><affiliation>Laboratoire d'Immunologie Moléculaire et Parasitologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><affiliation>Centre Condorcet 162, GISIR-ADERA, Avenue A. Schweitzer BP, 196 33608, Pessac, France</affiliation><affiliation>E-mail: daniel.moynet@immol.u-bordeaux2.fr</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.</namePart><namePart type="family">Londos-Gagliardi</namePart><affiliation>Laboratoire de Virologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="given">H.</namePart><namePart type="family">Bezian</namePart><affiliation>Laboratoire d'Immunologie Moléculaire et Parasitologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><affiliation>Centre Condorcet 162, GISIR-ADERA, Avenue A. Schweitzer BP, 196 33608, Pessac, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Vincendeau</namePart><affiliation>Laboratoire d'Immunologie Moléculaire et Parasitologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Fleury</namePart><affiliation>Laboratoire de Virologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">Guillemain</namePart><affiliation>Centre Condorcet 162, GISIR-ADERA, Avenue A. Schweitzer BP, 196 33608, Pessac, France</affiliation><affiliation>Laboratoire de Virologie, Université Victor Segalen Bordeaux2, 146 rue Léo Saignat, 33076, Bordeaux, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" 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>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateCreated encoding="w3cdtf">2001-07-25</dateCreated><dateIssued encoding="w3cdtf">2001-03-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies (mAbs). Using screening of phage displayed random peptide libraries we have characterized the binding epitopes of three mAbs directed against the surface envelope glycoprotein (gp46) of the human T-cell leukemia virus type I (HTLV-I). Two phage libraries, displaying random heptapeptides with or without flanking cysteine residues, were screened for binding to mAbs 7G5D8, DB4 and 4F5F6. The SSSSTPL consensus sequence isolated from constrained heptapeptide library defines the epitope recognized by DB4 mAb and corresponds to the exact region 249–252 of the virus sequence. The APPMLPH consensus sequence isolated from non constrained heptapeptide library defines the epitope recognized by 7G5D8 mAb and corresponds to the region 187–193 with a single amino acid substitution, methionine to leucine at position 190. The third consensus sequence LYWPHD isolated from constrained heptapeptide library defines the epitope recognized by 4F5F6 mAb. It corresponds to an epitope without direct equivalence with the virus sequence. The data presented here showed that 7G5D8 and DB4 mAbs are raised against linear epitopes while 4F5F6 mAb recognized a continoous topographic epitope.</abstract><subject lang="en"><genre>Key words</genre><topic>epitope mapping</topic><topic>gp46</topic><topic>HTLV-I</topic><topic>human retrovirus</topic><topic>peptide library</topic><topic>phage display</topic></subject><relatedItem type="host"><titleInfo><title>Letters in Peptide Science</title></titleInfo><titleInfo type="abbreviated"><title>Lett Pept Sci</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>Springer</publisher><dateIssued encoding="w3cdtf">2001-03-01</dateIssued><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Polymer Sciences</topic><topic>Biochemistry, general</topic><topic>Animal Anatomy / Morphology / Histology</topic></subject><identifier type="ISSN">0929-5666</identifier><identifier type="eISSN">1573-496X</identifier><identifier type="JournalID">10989</identifier><identifier type="IssueArticleCount">6</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2001</date><detail type="volume"><number>8</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="pages"><start>95</start><end>106</end></extent></part><recordInfo><recordOrigin>Kluwer Academic Publishers, 2002</recordOrigin></recordInfo></relatedItem><identifier type="istex">619B14AF51B66457962728F4F8F2764144E566C0</identifier><identifier type="ark">ark:/67375/VQC-Z2JLQ57G-8</identifier><identifier type="DOI">10.1007/BF02443610</identifier><identifier type="ArticleID">BF02443610</identifier><identifier type="ArticleID">Art5</identifier><accessCondition type="use and reproduction" contentType="copyright">Kluwer Academic Publishers, 2002</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Kluwer Academic Publishers, 2002</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Z2JLQ57G-8/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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