Conserved stem fragment from H3 influenza hemagglutinin elicits cross-clade neutralizing antibodies through stalk-targeted blocking of conformational change during membrane fusion.
Identifieur interne : 001B32 ( Ncbi/Merge ); précédent : 001B31; suivant : 001B33Conserved stem fragment from H3 influenza hemagglutinin elicits cross-clade neutralizing antibodies through stalk-targeted blocking of conformational change during membrane fusion.
Auteurs : Xin Gong [République populaire de Chine] ; He Yin [République populaire de Chine] ; Yuhua Shi [République populaire de Chine] ; Shanshan Guan [République populaire de Chine] ; Xiaoqiu He [République populaire de Chine] ; Lan Yang [République populaire de Chine] ; Yongjiao Yu [République populaire de Chine] ; Ziyu Kuai [République populaire de Chine] ; Chunlai Jiang [République populaire de Chine] ; Wei Kong [République populaire de Chine] ; Song Wang [République populaire de Chine] ; Yaming Shan [République populaire de Chine]Source :
- Immunology letters [ 1879-0542 ] ; 2016.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Anticorps antiviraux (métabolisme), Anticorps neutralisants (métabolisme), Cartographie épitopique, Conformation des protéines, Cristallographie aux rayons X, Déterminants antigéniques des lymphocytes B (), Déterminants antigéniques des lymphocytes B (génétique), Déterminants antigéniques des lymphocytes B (immunologie), Déterminants antigéniques des lymphocytes T (), Déterminants antigéniques des lymphocytes T (génétique), Déterminants antigéniques des lymphocytes T (immunologie), Femelle, Fusion membranaire, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (immunologie), Grippe humaine (immunologie), Humains, Infections à Orthomyxoviridae (immunologie), Simulation numérique, Souris, Souris de lignée BALB C, Sous-type H3N2 du virus de la grippe A (immunologie), Séquence conservée (génétique), Techniques de chimie combinatoire, Vaccins antigrippaux (immunologie).
- MESH :
- génétique : Déterminants antigéniques des lymphocytes B, Déterminants antigéniques des lymphocytes T, Séquence conservée.
- immunologie : Déterminants antigéniques des lymphocytes B, Déterminants antigéniques des lymphocytes T, Glycoprotéine hémagglutinine du virus influenza, Grippe humaine, Infections à Orthomyxoviridae, Sous-type H3N2 du virus de la grippe A, Vaccins antigrippaux.
- métabolisme : Anticorps antiviraux, Anticorps neutralisants.
- Alignement de séquences, Animaux, Cartographie épitopique, Conformation des protéines, Cristallographie aux rayons X, Déterminants antigéniques des lymphocytes B, Déterminants antigéniques des lymphocytes T, Femelle, Fusion membranaire, Glycoprotéine hémagglutinine du virus influenza, Humains, Simulation numérique, Souris, Souris de lignée BALB C, Techniques de chimie combinatoire.
English descriptors
- KwdEn :
- Animals, Antibodies, Neutralizing (metabolism), Antibodies, Viral (metabolism), Combinatorial Chemistry Techniques, Computer Simulation, Conserved Sequence (genetics), Crystallography, X-Ray, Epitope Mapping, Epitopes, B-Lymphocyte (chemistry), Epitopes, B-Lymphocyte (genetics), Epitopes, B-Lymphocyte (immunology), Epitopes, T-Lymphocyte (chemistry), Epitopes, T-Lymphocyte (genetics), Epitopes, T-Lymphocyte (immunology), Female, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Humans, Influenza A Virus, H3N2 Subtype (immunology), Influenza Vaccines (immunology), Influenza, Human (immunology), Membrane Fusion, Mice, Mice, Inbred BALB C, Orthomyxoviridae Infections (immunology), Protein Conformation, Sequence Alignment.
- MESH :
- chemical , chemistry : Epitopes, B-Lymphocyte, Epitopes, T-Lymphocyte, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Epitopes, B-Lymphocyte, Epitopes, T-Lymphocyte.
- chemical , immunology : Epitopes, B-Lymphocyte, Epitopes, T-Lymphocyte, Hemagglutinin Glycoproteins, Influenza Virus, Influenza Vaccines.
- chemical , metabolism : Antibodies, Neutralizing, Antibodies, Viral.
- genetics : Conserved Sequence.
- immunology : Influenza A Virus, H3N2 Subtype, Influenza, Human, Orthomyxoviridae Infections.
- Animals, Combinatorial Chemistry Techniques, Computer Simulation, Crystallography, X-Ray, Epitope Mapping, Female, Humans, Membrane Fusion, Mice, Mice, Inbred BALB C, Protein Conformation, Sequence Alignment.
Abstract
Currently available influenza vaccines typically fail to elicit/boost broadly neutralizing antibodies due to the mutability of virus sequences and conformational changes during protective immunity, thereby limiting their efficacy. This problem needs to be addressed by further understanding the mechanisms of neutralization and finding the desired neutralizing site during membrane fusion. This study specifically focused on viruses of the H3N2 subtype, which have persisted as a principal source of influenza-related morbidity and mortality in humans since the 1968 influenza pandemic. Through sequence alignment and epitope prediction, a series of highly conserved stem fragments (spanning 47 years) were found and coupled to the Keyhole Limpet Hemocyanin (KLH) protein. By application of a combinatorial display library and crystal structure modeling, a stem fragment immunogen, located at the turning point of the HA neck undergoing conformational change during membrane fusion with both B- and T-cell epitopes, was identified. After synthesis of the optimal stem fragment using a multiple antigen peptide (MAP) system, strong humoral immune responses and cross-clade neutralizing activities against strains from the H3 subtype of group 2 influenza viruses after animal immunizations were observed. By detection of nuclear protein immunofluorescence with acid bypass treatment, antisera raised against MAP4 immunogens of the stem fragment showed the potential to inhibit the conformational change of HA in stem-targeted virus neutralization. The identification of this conserved stem fragment provides great potential for exploitation of this site of vulnerability in therapeutic and vaccine design.
DOI: 10.1016/j.imlet.2016.02.006
PubMed: 26875772
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pubmed:26875772Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Conserved stem fragment from H3 influenza hemagglutinin elicits cross-clade neutralizing antibodies through stalk-targeted blocking of conformational change during membrane fusion.</title>
<author><name sortKey="Gong, Xin" sort="Gong, Xin" uniqKey="Gong X" first="Xin" last="Gong">Xin Gong</name>
<affiliation wicri:level="4"><nlm:affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</nlm:affiliation>
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<author><name sortKey="Yin, He" sort="Yin, He" uniqKey="Yin H" first="He" last="Yin">He Yin</name>
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<author><name sortKey="Shi, Yuhua" sort="Shi, Yuhua" uniqKey="Shi Y" first="Yuhua" last="Shi">Yuhua Shi</name>
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<author><name sortKey="Guan, Shanshan" sort="Guan, Shanshan" uniqKey="Guan S" first="Shanshan" last="Guan">Shanshan Guan</name>
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<author><name sortKey="He, Xiaoqiu" sort="He, Xiaoqiu" uniqKey="He X" first="Xiaoqiu" last="He">Xiaoqiu He</name>
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<author><name sortKey="Yang, Lan" sort="Yang, Lan" uniqKey="Yang L" first="Lan" last="Yang">Lan Yang</name>
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<placeName><settlement type="city">Changchun</settlement>
<region type="province">Jilin</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Yu, Yongjiao" sort="Yu, Yongjiao" uniqKey="Yu Y" first="Yongjiao" last="Yu">Yongjiao Yu</name>
<affiliation wicri:level="4"><nlm:affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin</wicri:regionArea>
<orgName type="university">Université de Jilin</orgName>
<placeName><settlement type="city">Changchun</settlement>
<region type="province">Jilin</region>
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<author><name sortKey="Kuai, Ziyu" sort="Kuai, Ziyu" uniqKey="Kuai Z" first="Ziyu" last="Kuai">Ziyu Kuai</name>
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<author><name sortKey="Jiang, Chunlai" sort="Jiang, Chunlai" uniqKey="Jiang C" first="Chunlai" last="Jiang">Chunlai Jiang</name>
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<orgName type="university">Université de Jilin</orgName>
<placeName><settlement type="city">Changchun</settlement>
<region type="province">Jilin</region>
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<author><name sortKey="Kong, Wei" sort="Kong, Wei" uniqKey="Kong W" first="Wei" last="Kong">Wei Kong</name>
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<orgName type="university">Université de Jilin</orgName>
<placeName><settlement type="city">Changchun</settlement>
<region type="province">Jilin</region>
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<author><name sortKey="Wang, Song" sort="Wang, Song" uniqKey="Wang S" first="Song" last="Wang">Song Wang</name>
<affiliation wicri:level="4"><nlm:affiliation>State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun, Jilin, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun, Jilin</wicri:regionArea>
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<author><name sortKey="Shan, Yaming" sort="Shan, Yaming" uniqKey="Shan Y" first="Yaming" last="Shan">Yaming Shan</name>
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<orgName type="university">Université de Jilin</orgName>
<placeName><settlement type="city">Changchun</settlement>
<region type="province">Jilin</region>
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<term>Déterminants antigéniques des lymphocytes B (immunologie)</term>
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<front><div type="abstract" xml:lang="en">Currently available influenza vaccines typically fail to elicit/boost broadly neutralizing antibodies due to the mutability of virus sequences and conformational changes during protective immunity, thereby limiting their efficacy. This problem needs to be addressed by further understanding the mechanisms of neutralization and finding the desired neutralizing site during membrane fusion. This study specifically focused on viruses of the H3N2 subtype, which have persisted as a principal source of influenza-related morbidity and mortality in humans since the 1968 influenza pandemic. Through sequence alignment and epitope prediction, a series of highly conserved stem fragments (spanning 47 years) were found and coupled to the Keyhole Limpet Hemocyanin (KLH) protein. By application of a combinatorial display library and crystal structure modeling, a stem fragment immunogen, located at the turning point of the HA neck undergoing conformational change during membrane fusion with both B- and T-cell epitopes, was identified. After synthesis of the optimal stem fragment using a multiple antigen peptide (MAP) system, strong humoral immune responses and cross-clade neutralizing activities against strains from the H3 subtype of group 2 influenza viruses after animal immunizations were observed. By detection of nuclear protein immunofluorescence with acid bypass treatment, antisera raised against MAP4 immunogens of the stem fragment showed the potential to inhibit the conformational change of HA in stem-targeted virus neutralization. The identification of this conserved stem fragment provides great potential for exploitation of this site of vulnerability in therapeutic and vaccine design.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>11</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2017</Year>
<Month>12</Month>
<Day>16</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0542</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>172</Volume>
<PubDate><Year>2016</Year>
<Month>04</Month>
</PubDate>
</JournalIssue>
<Title>Immunology letters</Title>
<ISOAbbreviation>Immunol. Lett.</ISOAbbreviation>
</Journal>
<ArticleTitle>Conserved stem fragment from H3 influenza hemagglutinin elicits cross-clade neutralizing antibodies through stalk-targeted blocking of conformational change during membrane fusion.</ArticleTitle>
<Pagination><MedlinePgn>11-20</MedlinePgn>
</Pagination>
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<ELocationID EIdType="pii" ValidYN="Y">S0165-2478(16)30015-3</ELocationID>
<Abstract><AbstractText>Currently available influenza vaccines typically fail to elicit/boost broadly neutralizing antibodies due to the mutability of virus sequences and conformational changes during protective immunity, thereby limiting their efficacy. This problem needs to be addressed by further understanding the mechanisms of neutralization and finding the desired neutralizing site during membrane fusion. This study specifically focused on viruses of the H3N2 subtype, which have persisted as a principal source of influenza-related morbidity and mortality in humans since the 1968 influenza pandemic. Through sequence alignment and epitope prediction, a series of highly conserved stem fragments (spanning 47 years) were found and coupled to the Keyhole Limpet Hemocyanin (KLH) protein. By application of a combinatorial display library and crystal structure modeling, a stem fragment immunogen, located at the turning point of the HA neck undergoing conformational change during membrane fusion with both B- and T-cell epitopes, was identified. After synthesis of the optimal stem fragment using a multiple antigen peptide (MAP) system, strong humoral immune responses and cross-clade neutralizing activities against strains from the H3 subtype of group 2 influenza viruses after animal immunizations were observed. By detection of nuclear protein immunofluorescence with acid bypass treatment, antisera raised against MAP4 immunogens of the stem fragment showed the potential to inhibit the conformational change of HA in stem-targeted virus neutralization. The identification of this conserved stem fragment provides great potential for exploitation of this site of vulnerability in therapeutic and vaccine design.</AbstractText>
<CopyrightInformation>Copyright © 2016 European Federation of Immunological Societies. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
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<ForeName>Xin</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yin</LastName>
<ForeName>He</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Yuhua</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
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<ForeName>Shanshan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
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<ForeName>Xiaoqiu</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
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<Initials>C</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China; Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
</Author>
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<ForeName>Wei</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China; Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, School of Life Sciences, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
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<ForeName>Song</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun, Jilin, China.</Affiliation>
</AffiliationInfo>
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<ForeName>Yaming</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>National Engineering Laboratory for AIDS Vaccine, School of Life Sciences, Jilin University, Changchun, Jilin, China; Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, School of Life Sciences, Jilin University, Changchun, Jilin, China. Electronic address: shanym@jlu.edu.cn.</Affiliation>
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<Month>02</Month>
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