Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses
Identifieur interne : 000132 ( Istex/Corpus ); 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 ; Zhe Yan ; Jonathan A. Shortt ; David D. Pollock ; Zhaohui Qian ; Kathryn V. Holmes ; Robert S. HodgesSource :
- 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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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></affiliation></author><author><name sortKey="Hirsch, Brooke" sort="Hirsch, Brooke" uniqKey="Hirsch B" first="Brooke" last="Hirsch">Brooke Hirsch</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</mods:affiliation></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><mods:affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</mods:affiliation></affiliation><affiliation><mods:affiliation>Molecular Cloning Laboratories (MCLAB), CA, 94080, San Francisco</mods:affiliation></affiliation></author><author><name sortKey="Shortt, Jonathan A" sort="Shortt, Jonathan A" uniqKey="Shortt J" first="Jonathan A." last="Shortt">Jonathan A. 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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></affiliation></author><author><name sortKey="Qian, Zhaohui" sort="Qian, Zhaohui" uniqKey="Qian Z" first="Zhaohui" last="Qian">Zhaohui Qian</name><affiliation><mods:affiliation>Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7, 100176, Beijing, China</mods:affiliation></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></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><mods:affiliation>E-mail: Robert.Hodges@ucdenver.edu</mods:affiliation></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><istex><corpusName>wiley</corpusName><author><json:item><name>Ziqing Jiang</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</json:string></affiliations></json:item><json:item><name>Lajos Gera</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</json:string></affiliations></json:item><json:item><name>Colin T. Mant</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</json:string></affiliations></json:item><json:item><name>Brooke Hirsch</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</json:string><json:string>Flagship Biosciences, CO, 80021, Westminster</json:string></affiliations></json:item><json:item><name>Zhe Yan</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</json:string><json:string>Molecular Cloning Laboratories (MCLAB), CA, 94080, San Francisco</json:string></affiliations></json:item><json:item><name>Jonathan A. 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Holmes</name><affiliations><json:string>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</json:string></affiliations></json:item><json:item><name>Robert S. Hodges</name><affiliations><json:string>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</json:string><json:string>E-mail: Robert.Hodges@ucdenver.edu</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>helical epitopes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>synthetic peptide vaccines</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>coiled‐coil immunogens</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>hemagglutinin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>influenza A viruses</value></json:item></subject><articleId><json:string>BIP22808</json:string></articleId><arkIstex>ark:/67375/WNG-31ZX07K4-H</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><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. 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xml:id="author-0000"><persName><forename type="first">Ziqing</forename><surname>Jiang</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Lajos</forename><surname>Gera</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Colin T.</forename><surname>Mant</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Brooke</forename><surname>Hirsch</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation><affiliation><orgName type="institution">Flagship Biosciences</orgName><address><settlement>Westminster</settlement><region>CO</region><postCode>80021</postCode></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Zhe</forename><surname>Yan</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation><affiliation><orgName type="institution">Molecular Cloning Laboratories (MCLAB)</orgName><address><settlement>San Francisco</settlement><region>CA</region><postCode>94080</postCode></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">Jonathan A.</forename><surname>Shortt</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0006"><persName><forename type="first">David D.</forename><surname>Pollock</surname></persName><affiliation><orgName type="division">Department of Biochemistry and Molecular Genetics</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0007"><persName><forename type="first">Zhaohui</forename><surname>Qian</surname></persName><affiliation><orgName type="institution">Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7</orgName><address><settlement>Beijing</settlement><postCode>100176</postCode><country key="CN" xml:lang="en">CHINA</country></address></affiliation><affiliation><orgName type="division">Department of Immunology and Microbiology</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0008"><persName><forename type="first">Kathryn V.</forename><surname>Holmes</surname></persName><affiliation><orgName type="division">Department of Immunology and Microbiology</orgName><orgName type="institution">University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><settlement>Aurora</settlement><region>CO</region><postCode>80045</postCode></address></affiliation></author><author xml:id="author-0009" role="corresp"><persName><forename type="first">Robert S.</forename><surname>Hodges</surname></persName><affiliation><orgName type="division">Department of Biochemistry and 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to="159">159</biblScope><biblScope unit="page-count">16</biblScope><date type="published" when="2016-03"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><encodingDesc><schemaRef type="ODD" url="https://xml-schema.delivery.istex.fr/tei-istex.odd"></schemaRef><appInfo><application ident="pub2tei" version="1.0.10" when="2019-12-20"><label>pub2TEI-ISTEX</label><desc>A set of style sheets for converting XML documents encoded in various scientific publisher formats into a common TEI format.
<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract style="main"><head>ABSTRACT</head><p>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.</p></abstract><textClass><keywords><term xml:id="bip22808-kwd-0001">helical epitopes</term><term xml:id="bip22808-kwd-0002">synthetic peptide vaccines</term><term xml:id="bip22808-kwd-0003">coiled‐coil immunogens</term><term xml:id="bip22808-kwd-0004">hemagglutinin</term><term xml:id="bip22808-kwd-0005">influenza A viruses</term></keywords><keywords rend="articleCategory"><term>Article</term></keywords><keywords rend="tocHeading1"><term>Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-31ZX07K4-H/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en" xml:id="bip22808"><header><publicationMeta level="product"><doi origin="wiley" registered="yes">10.1002/(ISSN)1097-0282a</doi><issn type="print">0006-3525</issn><issn type="electronic">1097-0282</issn><idGroup><id type="product" value="BIP"></id></idGroup><titleGroup><title type="main" sort="PEPTIDE SCIENCE">Peptide Science</title><title type="short">Biopolymers</title></titleGroup></publicationMeta><publicationMeta level="part" position="20"><doi>10.1002/bip.v106.2</doi><idGroup><id type="focusSection" value="1"></id></idGroup><titleGroup><title type="focusSection">Peptide Science</title></titleGroup><copyright ownership="publisher">© 2016 Wiley Periodicals, Inc.</copyright><numberingGroup><numbering type="journalVolume" number="106">106</numbering><numbering type="journalIssue">2</numbering></numberingGroup><coverDate startDate="2016-03">March 2016</coverDate></publicationMeta><publicationMeta level="unit" position="30" type="article" status="forIssue"><doi>10.1002/bip.22808</doi><idGroup><id type="unit" value="BIP22808"></id></idGroup><countGroup><count type="pageTotal" number="16"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Articles</title></titleGroup><copyright ownership="publisher">© 2016 Wiley Periodicals, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2015-09-24"></event><event type="manuscriptRevised" date="2015-12-29"></event><event type="manuscriptAccepted" date="2016-01-10"></event><event type="xmlCreated" agent="Cenveo Publisher Services" date="2016-01-28"></event><event type="publishedOnlineAccepted" date="2016-01-21"></event><event type="firstOnline" date="2016-03-22"></event><event type="publishedOnlineFinalForm" date="2016-03-22"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:5.0.6 mode:FullText" date="2017-02-10"></event></eventGroup><numberingGroup><numbering type="pageFirst">144</numbering><numbering type="pageLast">159</numbering></numberingGroup><correspondenceTo><i>Correspondence to</i>: Robert S. Hodges, Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, Aurora, CO 80045; e‐mail: <email>Robert.Hodges@ucdenver.edu</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:BIP.BIP22808.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses</title><title type="short">Platform Technology to Generate Broadly Cross‐reactive Antibodies</title><title type="shortAuthors">Jiang et al.</title></titleGroup><creators><creator affiliationRef="#bip22808-aff-0001" creatorRole="author" xml:id="bip22808-cr-0001"><personName><givenNames>Ziqing</givenNames><familyName>Jiang</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001" creatorRole="author" xml:id="bip22808-cr-0002"><personName><givenNames>Lajos</givenNames><familyName>Gera</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001" creatorRole="author" xml:id="bip22808-cr-0003"><personName><givenNames>Colin T.</givenNames><familyName>Mant</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001 #bip22808-aff-0002" creatorRole="author" xml:id="bip22808-cr-0004"><personName><givenNames>Brooke</givenNames><familyName>Hirsch</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001 #bip22808-aff-0003" creatorRole="author" xml:id="bip22808-cr-0005"><personName><givenNames>Zhe</givenNames><familyName>Yan</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001" creatorRole="author" xml:id="bip22808-cr-0008"><personName><givenNames>Jonathan A.</givenNames><familyName>Shortt</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001" creatorRole="author" xml:id="bip22808-cr-0009"><personName><givenNames>David D.</givenNames><familyName>Pollock</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0004 #bip22808-aff-0005" creatorRole="author" xml:id="bip22808-cr-0006"><personName><givenNames>Zhaohui</givenNames><familyName>Qian</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0005" creatorRole="author" xml:id="bip22808-cr-0007"><personName><givenNames>Kathryn V.</givenNames><familyName>Holmes</familyName></personName></creator><creator affiliationRef="#bip22808-aff-0001" corresponding="yes" creatorRole="author" xml:id="bip22808-cr-0010"><personName><givenNames>Robert S.</givenNames><familyName>Hodges</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="US" type="organization" xml:id="bip22808-aff-0001"><orgDiv>Department of Biochemistry and Molecular Genetics</orgDiv><orgName>University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><city>Aurora</city><countryPart>CO</countryPart><postCode>80045</postCode></address></affiliation><affiliation countryCode="US" type="organization" xml:id="bip22808-aff-0002"><orgName>Flagship Biosciences</orgName><address><city>Westminster</city><countryPart>CO</countryPart><postCode>80021</postCode></address></affiliation><affiliation countryCode="US" type="organization" xml:id="bip22808-aff-0003"><orgName>Molecular Cloning Laboratories (MCLAB)</orgName><address><city>San Francisco</city><countryPart>CA</countryPart><postCode>94080</postCode></address></affiliation><affiliation countryCode="CN" type="organization" xml:id="bip22808-aff-0004"><orgName>Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7</orgName><address><city>Beijing</city><postCode>100176</postCode><country>China</country></address></affiliation><affiliation countryCode="US" type="organization" xml:id="bip22808-aff-0005"><orgDiv>Department of Immunology and Microbiology</orgDiv><orgName>University of Colorado, Anschutz Medical Campus, School of Medicine</orgName><address><city>Aurora</city><countryPart>CO</countryPart><postCode>80045</postCode></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="bip22808-kwd-0001">helical epitopes</keyword><keyword xml:id="bip22808-kwd-0002">synthetic peptide vaccines</keyword><keyword xml:id="bip22808-kwd-0003">coiled‐coil immunogens</keyword><keyword xml:id="bip22808-kwd-0004">hemagglutinin</keyword><keyword xml:id="bip22808-kwd-0005">influenza A viruses</keyword></keywordGroup><fundingInfo><fundingAgency>PeptiVir, Inc., State of Colorado; University of Colorado Technology Transfer Office Bioscience Discovery Evaluation Grant Program; John Stewart Endowed Chair in Peptide Chemistry to R.S.H.
</fundingAgency></fundingInfo><abstractGroup><abstract type="main"><title type="main">ABSTRACT</title><p>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.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="bip22808-note-0002"><p>This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of any preprints from the past two calendar years by emailing the Biopolymers editorial office at <email>biopolymers@wiley.com</email>.</p></note><note xml:id="bip22808-note-0001"><p>Author Contributions: Robert S. Hodges planned and organized the study including peptide design and was responsible for the manuscript writing. Ziqing Jiang was involved in peptide synthesis using Fmoc‐chemistry, peptide purification, ELISA evaluation of antibody cross‐reactivity to HA proteins and biophysical characterization of immunogens. Lajos Gera was involved in large scale synthesis of peptide immunogens using Boc‐chemistry. Colin Mant was responsible for the large scale reversed‐phase HPLC purification of peptide immunogens. Brooke Hirsch was involved in preliminary studies on epitope selection which involved small scale peptide synthesis, purification, biophysical characterization and antibody evaluation by ELISA. Zhe Yan developed the methodology for conjugation of peptide immunogens to protein carriers, KLH and BSA, purification of IgG from rabbit polyclonal sera and ELISA evaluation of purified antibodies. Zhaohui Qian and Kathryn Holmes were responsible for the initial <i>in vivo</i> study in mice to demonstrate protection against lethal influenza virus infection by passive immunization with rabbit IgG to one of our peptide immunogens. Jonathan Shortt and David Pollock provided the analysis of all hemagglutinin sequences from H1N1, H5N1 and H3N2.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Platform Technology to Generate Broadly Cross‐reactive Antibodies</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Platform technology to generate broadly cross‐reactive antibodies to α‐helical epitopes in hemagglutinin proteins from influenza A viruses</title></titleInfo><name type="personal"><namePart type="given">Ziqing</namePart><namePart type="family">Jiang</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lajos</namePart><namePart type="family">Gera</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Colin T.</namePart><namePart type="family">Mant</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Brooke</namePart><namePart type="family">Hirsch</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</affiliation><affiliation>Flagship Biosciences, CO, 80021, Westminster</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Zhe</namePart><namePart type="family">Yan</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, 80045, Aurora, CO</affiliation><affiliation>Molecular Cloning Laboratories (MCLAB), CA, 94080, San Francisco</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jonathan A.</namePart><namePart type="family">Shortt</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David D.</namePart><namePart type="family">Pollock</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Zhaohui</namePart><namePart type="family">Qian</namePart><affiliation>Institute of Pathogen Biology at Chinese Academy of Medical Sciences, Yi Zhuang DiShengBeiLu, BeiGongDa RuanJianYuan, Bldg#7, 100176, Beijing, China</affiliation><affiliation>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kathryn V.</namePart><namePart type="family">Holmes</namePart><affiliation>Department of Immunology and Microbiology, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert S.</namePart><namePart type="family">Hodges</namePart><affiliation>Department of Biochemistry and Molecular Genetics, University of Colorado, Anschutz Medical Campus, School of Medicine, CO, 80045, Aurora</affiliation><affiliation>E-mail: Robert.Hodges@ucdenver.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2016-03</dateIssued><dateCreated encoding="w3cdtf">2016-01-28</dateCreated><dateCaptured encoding="w3cdtf">2015-09-24</dateCaptured><dateValid encoding="w3cdtf">2016-01-10</dateValid><copyrightDate encoding="w3cdtf">2016</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><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.</abstract><note type="funding">PeptiVir, Inc., State of Colorado; University of Colorado Technology Transfer Office Bioscience Discovery Evaluation Grant Program; John Stewart Endowed Chair in Peptide Chemistry to R.S.H.</note><subject><genre>keywords</genre><topic>helical epitopes</topic><topic>synthetic peptide vaccines</topic><topic>coiled‐coil immunogens</topic><topic>hemagglutinin</topic><topic>influenza A viruses</topic></subject><relatedItem type="host"><titleInfo><title>Peptide Science</title></titleInfo><titleInfo type="abbreviated"><title>Biopolymers</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><subject><genre>article-category</genre><topic>Article</topic><topic>Articles</topic></subject><identifier type="ISSN">0006-3525</identifier><identifier type="eISSN">1097-0282</identifier><identifier type="DOI">10.1002/(ISSN)1097-0282a</identifier><identifier type="PublisherID">BIP</identifier><part><date>2016</date><detail type="volume"><caption>vol.</caption><number>106</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>144</start><end>159</end><total>16</total></extent></part></relatedItem><relatedItem type="references" displayLabel="bip22808-cit-0001"><titleInfo><title>WHO. 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