Optimization of an enzyme-linked lectin assay suitable for rapid antigenic characterization of the neuraminidase of human influenza A(H3N2) viruses
Identifieur interne : 000855 ( Pmc/Curation ); précédent : 000854; suivant : 000856Optimization of an enzyme-linked lectin assay suitable for rapid antigenic characterization of the neuraminidase of human influenza A(H3N2) viruses
Auteurs : Kim Westgeest [Pays-Bas] ; Theo M. Bestebroer [Pays-Bas] ; Monique I. J. Spronken [Pays-Bas] ; Jin Gao [États-Unis] ; Laura Couzens [États-Unis] ; Albert D. M. E. Osterhaus [Pays-Bas] ; Maryna Eichelberger [États-Unis] ; Ron A. M. Fouchier [Pays-Bas] ; Miranda De Graaf [Pays-Bas]Source :
- Journal of virological methods [ 0166-0934 ] ; 2015.
Abstract
Antibodies to neuraminidase (NA), the second most abundant surface protein of the influenza virus, contribute to protection against influenza virus infection. Although traditional and miniaturized thiobarbituric acid (TBA) neuraminidase inhibition (NI) assays have been successfully used to characterize the antigenic properties of NA, these methods are cumbersome and not easily amendable to rapid screening. An additional difficulty of the NI assay is the interference by hemagglutinin (HA)-specific antibodies. To prevent interference of HA-specific antibodies, most NI assays are performed with recombinant viruses containing a mismatched HA. However, generation of these viruses is time consuming and unsuitable for large-scale surveillance. The feasibility of using the recently developed enzyme-linked lectin assay (ELLA) to evaluate the antigenic relatedness of NA of wild type A(H3N2) viruses was assessed. Rather than using recombinant viruses, wild type A(H3N2) viruses were used as antigen with ferret sera elicited against recombinant viruses with a mismatched HA. In this study, details of the critical steps that are needed to modify and optimize the NI ELLA in a format that is reproducible, highly sensitive, and useful for influenza virus surveillance to monitor antigenic drift of NA are provided.
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DOI: 10.1016/j.jviromet.2015.02.014
PubMed: 25712563
PubMed Central: 4380634
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Bestebroer</name><affiliation wicri:level="1"><nlm:aff id="A1">Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Viroscience, Erasmus Medical Center, Rotterdam</wicri:regionArea></affiliation></author><author><name sortKey="Spronken, Monique I J" sort="Spronken, Monique I J" uniqKey="Spronken M" first="Monique I. J." last="Spronken">Monique I. J. Spronken</name><affiliation wicri:level="1"><nlm:aff id="A1">Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Viroscience, Erasmus Medical Center, Rotterdam</wicri:regionArea></affiliation></author><author><name sortKey="Gao, Jin" sort="Gao, Jin" uniqKey="Gao J" first="Jin" last="Gao">Jin Gao</name><affiliation wicri:level="1"><nlm:aff id="A2">Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993</wicri:regionArea></affiliation></author><author><name sortKey="Couzens, Laura" sort="Couzens, Laura" uniqKey="Couzens L" first="Laura" last="Couzens">Laura Couzens</name><affiliation wicri:level="1"><nlm:aff id="A2">Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993</wicri:regionArea></affiliation></author><author><name sortKey="Osterhaus, Albert D M E" sort="Osterhaus, Albert D M E" uniqKey="Osterhaus A" first="Albert D. 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Osterhaus</name><affiliation wicri:level="1"><nlm:aff id="A1">Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Viroscience, Erasmus Medical Center, Rotterdam</wicri:regionArea></affiliation></author><author><name sortKey="Eichelberger, Maryna" sort="Eichelberger, Maryna" uniqKey="Eichelberger M" first="Maryna" last="Eichelberger">Maryna Eichelberger</name><affiliation wicri:level="1"><nlm:aff id="A2">Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993</wicri:regionArea></affiliation></author><author><name sortKey="Fouchier, Ron A M" sort="Fouchier, Ron A M" uniqKey="Fouchier R" first="Ron A. M." last="Fouchier">Ron A. M. Fouchier</name><affiliation wicri:level="1"><nlm:aff id="A1">Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Viroscience, Erasmus Medical Center, Rotterdam</wicri:regionArea></affiliation></author><author><name sortKey="De Graaf, Miranda" sort="De Graaf, Miranda" uniqKey="De Graaf M" first="Miranda" last="De Graaf">Miranda De Graaf</name><affiliation wicri:level="1"><nlm:aff id="A1">Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</nlm:aff><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Department of Viroscience, Erasmus Medical Center, Rotterdam</wicri:regionArea></affiliation></author></analytic><series><title level="j">Journal of virological methods</title><idno type="ISSN">0166-0934</idno><idno type="eISSN">1879-0984</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Antibodies to neuraminidase (NA), the second most abundant surface protein of the influenza virus, contribute to protection against influenza virus infection. Although traditional and miniaturized thiobarbituric acid (TBA) neuraminidase inhibition (NI) assays have been successfully used to characterize the antigenic properties of NA, these methods are cumbersome and not easily amendable to rapid screening. An additional difficulty of the NI assay is the interference by hemagglutinin (HA)-specific antibodies. To prevent interference of HA-specific antibodies, most NI assays are performed with recombinant viruses containing a mismatched HA. However, generation of these viruses is time consuming and unsuitable for large-scale surveillance. The feasibility of using the recently developed enzyme-linked lectin assay (ELLA) to evaluate the antigenic relatedness of NA of wild type A(H3N2) viruses was assessed. Rather than using recombinant viruses, wild type A(H3N2) viruses were used as antigen with ferret sera elicited against recombinant viruses with a mismatched HA. In this study, details of the critical steps that are needed to modify and optimize the NI ELLA in a format that is reproducible, highly sensitive, and useful for influenza virus surveillance to monitor antigenic drift of NA are provided.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">8005839</journal-id><journal-id journal-id-type="pubmed-jr-id">4621</journal-id><journal-id journal-id-type="nlm-ta">J Virol Methods</journal-id><journal-id journal-id-type="iso-abbrev">J. Virol. Methods</journal-id><journal-title-group><journal-title>Journal of virological methods</journal-title></journal-title-group><issn pub-type="ppub">0166-0934</issn><issn pub-type="epub">1879-0984</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25712563</article-id><article-id pub-id-type="pmc">4380634</article-id><article-id pub-id-type="doi">10.1016/j.jviromet.2015.02.014</article-id><article-id pub-id-type="manuscript">NIHMS666577</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Optimization of an enzyme-linked lectin assay suitable for rapid antigenic characterization of the neuraminidase of human influenza A(H3N2) viruses</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Westgeest</surname><given-names>Kim</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Bestebroer</surname><given-names>Theo M.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Spronken</surname><given-names>Monique I.J.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Gao</surname><given-names>Jin</given-names></name><xref ref-type="aff" rid="A2">b</xref></contrib><contrib contrib-type="author"><name><surname>Couzens</surname><given-names>Laura</given-names></name><xref ref-type="aff" rid="A2">b</xref></contrib><contrib contrib-type="author"><name><surname>Osterhaus</surname><given-names>Albert D.M.E.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Eichelberger</surname><given-names>Maryna</given-names></name><xref ref-type="aff" rid="A2">b</xref></contrib><contrib contrib-type="author"><name><surname>Fouchier</surname><given-names>Ron A.M.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>de Graaf</surname><given-names>Miranda</given-names></name><email>m.degraaf@erasmusmc.nl</email><xref ref-type="aff" rid="A1">a</xref><xref rid="FN1" ref-type="author-notes">*</xref></contrib></contrib-group><aff id="A1"><label>a</label>Department of Viroscience, Erasmus Medical Center, Rotterdam, The Netherlands</aff><aff id="A2"><label>b</label>Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD 20993, USA</aff><author-notes><corresp id="FN1"><label>*</label>Corresponding author. Tel.: +31 107044067; fax: +31 107044760</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>20</day><month>3</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>21</day><month>2</month><year>2015</year></pub-date><pub-date pub-type="ppub"><day>1</day><month>6</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>6</month><year>2016</year></pub-date><volume>217</volume><fpage>55</fpage><lpage>63</lpage><pmc-comment>elocation-id from pubmed: 10.1016/j.jviromet.2015.02.014</pmc-comment>
<permissions><copyright-statement>© 2015 Published by Elsevier B.V.</copyright-statement><copyright-year>2015</copyright-year></permissions><abstract><p id="P1">Antibodies to neuraminidase (NA), the second most abundant surface protein of the influenza virus, contribute to protection against influenza virus infection. Although traditional and miniaturized thiobarbituric acid (TBA) neuraminidase inhibition (NI) assays have been successfully used to characterize the antigenic properties of NA, these methods are cumbersome and not easily amendable to rapid screening. An additional difficulty of the NI assay is the interference by hemagglutinin (HA)-specific antibodies. To prevent interference of HA-specific antibodies, most NI assays are performed with recombinant viruses containing a mismatched HA. However, generation of these viruses is time consuming and unsuitable for large-scale surveillance. The feasibility of using the recently developed enzyme-linked lectin assay (ELLA) to evaluate the antigenic relatedness of NA of wild type A(H3N2) viruses was assessed. Rather than using recombinant viruses, wild type A(H3N2) viruses were used as antigen with ferret sera elicited against recombinant viruses with a mismatched HA. In this study, details of the critical steps that are needed to modify and optimize the NI ELLA in a format that is reproducible, highly sensitive, and useful for influenza virus surveillance to monitor antigenic drift of NA are provided.</p></abstract><kwd-group><kwd>Influenza</kwd><kwd>Neuraminidase</kwd><kwd>Antigenic drift</kwd><kwd>ELLA</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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