Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus
Identifieur interne : 000D59 ( Istex/Corpus ); précédent : 000D58; suivant : 000D60Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus
Auteurs : A. I. Klimov ; S. G. Markushin ; S. Prösch ; V. P. Ginzburg ; H. Heider ; A. M. Heider ; C. Schröeder ; R. G. WebsterSource :
- Archives of Virology [ 0304-8608 ] ; 1992-03-01.
English descriptors
- Teeft :
- Amantadine, Amino, Amino acid substitutions, Antigenic, Antigenic sites, Antigenic specificities, Antigenic specificity, Arch virol, Different positions, Drug resistance, Fowl, Fowl plague virus, Haemagglutinating, Haemagglutinating activity, Haemagglutinin, Heider, Influenza, Influenza virus, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutant, Mutation, Norakin, Rimantadine, Substitution, Virol, Virus, Virus strains.
Abstract
Summary: Norakin-resistant (NR) mutants of fowl plague virus (A/FPV/Wey-bridge, H7N7) have 1 to 2 (in one instance 3) amino acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. This potential effect should be taken into account when antiviral substances directed to surface influenza virus antigens are being developed for use as antiviral drugs.
Url:
DOI: 10.1007/BF01314632
Links to Exploration step
ISTEX:0D9675E47FC37B62387AF508383665FC9807AFE2Le document en format XML
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Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. 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acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. 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TocLevels="0"><VolumeIDStart>124</VolumeIDStart><VolumeIDEnd>124</VolumeIDEnd><VolumeIssueCount>4</VolumeIssueCount></VolumeInfo><Issue IssueType="Combined"><IssueInfo TocLevels="0"><IssueIDStart>1</IssueIDStart><IssueIDEnd>2</IssueIDEnd><IssueArticleCount>19</IssueArticleCount><IssueHistory><CoverDate><DateString>1992</DateString><Year>1992</Year><Month>3</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1992</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art13"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF01314632</ArticleID><ArticleDOI>10.1007/BF01314632</ArticleDOI><ArticleSequenceNumber>13</ArticleSequenceNumber><ArticleTitle Language="En">Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus</ArticleTitle><ArticleCategory>Original Papers</ArticleCategory><ArticleFirstPage>147</ArticleFirstPage><ArticleLastPage>155</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2005</Year><Month>3</Month><Day>1</Day></RegistrationDate><Received><Year>1991</Year><Month>4</Month><Day>22</Day></Received><Accepted><Year>1991</Year><Month>8</Month><Day>6</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1992</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>705</JournalID><VolumeIDStart>124</VolumeIDStart><VolumeIDEnd>124</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>2</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>I.</GivenName><FamilyName>Klimov</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>S.</GivenName><GivenName>G.</GivenName><FamilyName>Markushin</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>S.</GivenName><FamilyName>Prösch</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>V.</GivenName><GivenName>P.</GivenName><FamilyName>Ginzburg</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>H.</GivenName><FamilyName>Heider</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>M.</GivenName><FamilyName>Heider</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>C.</GivenName><FamilyName>Schröeder</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>R.</GivenName><GivenName>G.</GivenName><FamilyName>Webster</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Research Institute for Viral Preparations</OrgDivision><OrgName>Academy of Medical Sciences of the U.S.S.R.</OrgName><OrgAddress><City>Moscow</City><Country>USSR</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Institute of Virology</OrgDivision><OrgName>Humboldt University School of Medicine (Charité)</OrgName><OrgAddress><City>Berlin</City><Country>Federal Republic of Germany</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Department of Virology and Molecular Biology</OrgDivision><OrgName>St. Jude Children's Research Hospital</OrgName><OrgAddress><City>Memphis</City><State>Tennessee</State><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>Norakin-resistant (NR) mutants of fowl plague virus (A/FPV/Wey-bridge, H7N7) have 1 to 2 (in one instance 3) amino acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. This potential effect should be taken into account when antiviral substances directed to surface influenza virus antigens are being developed for use as antiviral drugs.</Para></Abstract></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Relation between drug resistance and antigenicity among norakin-resistant mutants of influenza A (fowl plague) virus</title></titleInfo><name type="personal"><namePart type="given">A.</namePart><namePart type="given">I.</namePart><namePart type="family">Klimov</namePart><affiliation>Research Institute for Viral Preparations, Academy of Medical Sciences of the U.S.S.R., Moscow, USSR</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="given">G.</namePart><namePart type="family">Markushin</namePart><affiliation>Research Institute for Viral Preparations, Academy of Medical Sciences of the U.S.S.R., Moscow, USSR</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Prösch</namePart><affiliation>Institute of Virology, Humboldt University School of Medicine (Charité), Berlin, Federal Republic of Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.</namePart><namePart type="given">P.</namePart><namePart type="family">Ginzburg</namePart><affiliation>Research Institute for Viral Preparations, Academy of Medical Sciences of the U.S.S.R., Moscow, USSR</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Heider</namePart><affiliation>Institute of Virology, Humboldt University School of Medicine (Charité), Berlin, Federal Republic of Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="given">M.</namePart><namePart type="family">Heider</namePart><affiliation>Research Institute for Viral Preparations, Academy of Medical Sciences of the U.S.S.R., Moscow, USSR</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">C.</namePart><namePart type="family">Schröeder</namePart><affiliation>Institute of Virology, Humboldt University School of Medicine (Charité), Berlin, Federal Republic of Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="given">G.</namePart><namePart type="family">Webster</namePart><affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA</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>Springer-Verlag</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateCreated encoding="w3cdtf">1991-04-22</dateCreated><dateIssued encoding="w3cdtf">1992-03-01</dateIssued><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: Norakin-resistant (NR) mutants of fowl plague virus (A/FPV/Wey-bridge, H7N7) have 1 to 2 (in one instance 3) amino acid substitutions in different positions of the heavy (HA 1) and/or light (HA 2) subunits of the haemagglutinin (HA) molecule. Investigation of NR mutants using the haemagglutination inhibition test with monoclonal antibodies (MAb) to the HA of A/seal/Massachusetts/80 (H7N7) virus revealed that one of the mutants (NR 1) differs antigenically from the wild-type fowl plague virus: its haemagglutination was not inhibited by MAb 55/2 and 58/6. By contrast, MAb-resistant (escape) mutants, selected from the wild-type fowl plague virus under pressure from MAb 55/2 or 58/6, showed reduced drug sensitivity. These findings suggest a possibility of correlation between alteration of influenza virus antigenicity and change of its sensitivity to drugs whose target is the haemagglutinin. This potential effect should be taken into account when antiviral substances directed to surface influenza virus antigens are being developed for use as antiviral drugs.</abstract><note>Original Papers</note><relatedItem type="host"><titleInfo><title>Archives of Virology</title></titleInfo><titleInfo type="abbreviated"><title>Archives of Virology</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">1992-03-01</dateIssued><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><subject><genre>Biomedicine</genre><topic>Medical Microbiology</topic><topic>Virology</topic><topic>Infectious Diseases</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="IssueArticleCount">19</identifier><identifier type="VolumeIssueCount">4</identifier><part><date>1992</date><detail type="volume"><number>124</number><caption>vol.</caption></detail><detail type="issue"><number>1-2</number><caption>no.</caption></detail><extent unit="pages"><start>147</start><end>155</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1992</recordOrigin></recordInfo></relatedItem><identifier type="istex">0D9675E47FC37B62387AF508383665FC9807AFE2</identifier><identifier type="ark">ark:/67375/1BB-DDP844KG-0</identifier><identifier type="DOI">10.1007/BF01314632</identifier><identifier type="ArticleID">BF01314632</identifier><identifier type="ArticleID">Art13</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 1992</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>Springer-Verlag, 1992</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-DDP844KG-0/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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