Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses
Identifieur interne : 000132 ( Istex/Curation ); précédent : 000131; suivant : 000133Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses
Auteurs : Ziqing Jiang ; Lajos Gera ; Colin T. Mant ; Brooke Hirsch [États-Unis] ; Zhe Yan [États-Unis] ; Jonathan A. Shortt ; David D. Pollock ; Zhaohui Qian [République populaire de Chine] ; Kathryn V. Holmes ; Robert S. Hodges [États-Unis]Source :
- Peptide Science [ 0006-3525 ] ; 2016-03.
Abstract
We have utilized a de novo designed two‐stranded α‐helical coiled‐coil template to display conserved α‐helical epitopes from the stem region of hemagglutinin (HA) glycoproteins of influenza A. The immunogens have all the surface‐exposed residues of the native α‐helix in the native HA protein of interest displayed on the surface of the two‐stranded α‐helical coiled‐coil template. This template when used as an immunogen elicits polyclonal antibodies which bind to the α‐helix in the native protein. We investigated the highly conserved sequence region 421–476 of HA by inserting 21 or 28 residue sequences from this region into our template. The cross‐reactivity of the resulting rabbit polyclonal antibodies prepared to these immunogens was determined using a series of HA proteins from H1N1, H2N2, H3N2, H5N1, H7N7, and H7N9 virus strains which are representative of Group 1 and Group 2 virus subtypes of influenza A. Antibodies from region 449–476 were Group 1 specific. Antibodies to region 421–448 showed the greatest degree of cross‐reactivity to Group 1 and Group 2 and suggested that this region has a great potential as a “universal” synthetic peptide vaccine for influenza A. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 144–159, 2016.
Url:
DOI: 10.1002/bip.22808
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Ziqing Jiang<affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation>Le document en format XML
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Hodges</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation><affiliation wicri:level="1"><mods:affiliation>E-mail: Robert.Hodges@ucdenver.edu</mods:affiliation><country wicri:rule="url">États-Unis</country></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:BDC18B48D59DE81DAA5DC7D9B4834C10ACAA4827</idno><date when="2016" year="2016">2016</date><idno type="doi">10.1002/bip.22808</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-31ZX07K4-H/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000132</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000132</idno><idno type="wicri:Area/Istex/Curation">000132</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses</title><author><name sortKey="Jiang, Ziqing" sort="Jiang, Ziqing" uniqKey="Jiang Z" first="Ziqing" last="Jiang">Ziqing Jiang</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Gera, Lajos" sort="Gera, Lajos" uniqKey="Gera L" first="Lajos" last="Gera">Lajos Gera</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Mant, Colin T" sort="Mant, Colin T" uniqKey="Mant C" first="Colin T." last="Mant">Colin T. Mant</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Hirsch, Brooke" sort="Hirsch, Brooke" uniqKey="Hirsch B" first="Brooke" last="Hirsch">Brooke Hirsch</name><affiliation wicri:level="2"><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Colorado</region></placeName><wicri:cityArea>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora</wicri:cityArea></affiliation><affiliation><mods:affiliation>Flagship Biosciences, CO, 80021, Westminster</mods:affiliation></affiliation></author><author><name sortKey="Yan, Zhe" sort="Yan, Zhe" uniqKey="Yan Z" first="Zhe" last="Yan">Zhe Yan</name><affiliation wicri:level="2"><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Colorado</region></placeName><wicri:cityArea>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora</wicri:cityArea></affiliation><affiliation wicri:level="3"><mods:affiliation>Molecular Cloning Laboratories (MCLAB), CA, 94080, San Francisco</mods:affiliation><country>États-Unis</country><placeName><settlement type="city">San Francisco</settlement><region type="state">Californie</region></placeName><wicri:orgArea>Molecular Cloning Laboratories (MCLAB), CA, 94080</wicri:orgArea></affiliation></author><author><name sortKey="Shortt, Jonathan A" sort="Shortt, Jonathan A" uniqKey="Shortt J" first="Jonathan A." last="Shortt">Jonathan A. Shortt</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Pollock, David D" sort="Pollock, David D" uniqKey="Pollock D" first="David D." last="Pollock">David D. Pollock</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Qian, Zhaohui" sort="Qian, Zhaohui" uniqKey="Qian Z" first="Zhaohui" last="Qian">Zhaohui Qian</name><affiliation wicri:level="1"><mods:affiliation>Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7, 100176, Beijing, China</mods:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7, 100176, Beijing</wicri:regionArea></affiliation><affiliation><mods:affiliation>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation></affiliation></author><author><name sortKey="Holmes, Kathryn V" sort="Holmes, Kathryn V" uniqKey="Holmes K" first="Kathryn V." last="Holmes">Kathryn V. Holmes</name><affiliation><mods:affiliation>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation><wicri:noCountry code="subField">Aurora</wicri:noCountry></affiliation></author><author><name sortKey="Hodges, Robert S" sort="Hodges, Robert S" uniqKey="Hodges R" first="Robert S." last="Hodges">Robert S. Hodges</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</mods:affiliation></affiliation><affiliation wicri:level="1"><mods:affiliation>E-mail: Robert.Hodges@ucdenver.edu</mods:affiliation><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Peptide Science</title><title level="j" type="alt">PEPTIDE SCIENCE</title><idno type="ISSN">0006-3525</idno><idno type="eISSN">1097-0282</idno><imprint><biblScope unit="vol">106</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="144">144</biblScope><biblScope unit="page" to="159">159</biblScope><biblScope unit="page-count">16</biblScope><date type="published" when="2016-03">2016-03</date></imprint><idno type="ISSN">0006-3525</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3525</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">We have utilized a de novo designed two‐stranded α‐helical coiled‐coil template to display conserved α‐helical epitopes from the stem region of hemagglutinin (HA) glycoproteins of influenza A. The immunogens have all the surface‐exposed residues of the native α‐helix in the native HA protein of interest displayed on the surface of the two‐stranded α‐helical coiled‐coil template. This template when used as an immunogen elicits polyclonal antibodies which bind to the α‐helix in the native protein. We investigated the highly conserved sequence region 421–476 of HA by inserting 21 or 28 residue sequences from this region into our template. The cross‐reactivity of the resulting rabbit polyclonal antibodies prepared to these immunogens was determined using a series of HA proteins from H1N1, H2N2, H3N2, H5N1, H7N7, and H7N9 virus strains which are representative of Group 1 and Group 2 virus subtypes of influenza A. Antibodies from region 449–476 were Group 1 specific. Antibodies to region 421–448 showed the greatest degree of cross‐reactivity to Group 1 and Group 2 and suggested that this region has a great potential as a “universal” synthetic peptide vaccine for influenza A. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 144–159, 2016.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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