A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin
Identifieur interne : 000052 ( 1957/Analysis ); précédent : 000051; suivant : 000053A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin
Auteurs : Rui Xu [États-Unis] ; Jens C. Krause [États-Unis] ; Ryan Mcbride [États-Unis] ; James C. Paulson [États-Unis] ; James E. Crowe [États-Unis] ; Ian A. Wilson [États-Unis]Source :
- Nature structural & molecular biology [ 1545-9993 ] ; 2013.
Descripteurs français
- KwdFr :
- Anticorps antiviraux (génétique), Anticorps antiviraux (immunologie), Anticorps neutralisants (), Anticorps neutralisants (immunologie), Complexe antigène-anticorps, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Fragments Fab d'immunoglobuline (), Fragments Fab d'immunoglobuline (immunologie), Fragments Fab d'immunoglobuline (métabolisme), Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (immunologie), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Humains, Motifs d'acides aminés, Mutation, Sites de fixation, Sous-type H2N2 du virus de la grippe A (immunologie), Séquence d'acides aminés, Tryptophane (immunologie), Tryptophane (métabolisme), Tyrosine (métabolisme), Épitopes.
- MESH :
- génétique : Anticorps antiviraux.
- immunologie : Anticorps antiviraux, Anticorps neutralisants, Fragments Fab d'immunoglobuline, Glycoprotéine hémagglutinine du virus influenza, Sous-type H2N2 du virus de la grippe A, Tryptophane.
- métabolisme : Fragments Fab d'immunoglobuline, Glycoprotéine hémagglutinine du virus influenza, Tryptophane, Tyrosine.
- Anticorps neutralisants, Complexe antigène-anticorps, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Fragments Fab d'immunoglobuline, Glycoprotéine hémagglutinine du virus influenza, Humains, Motifs d'acides aminés, Mutation, Sites de fixation, Séquence d'acides aminés, Épitopes.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Antibodies, Neutralizing (chemistry), Antibodies, Neutralizing (immunology), Antibodies, Viral (genetics), Antibodies, Viral (immunology), Antigen-Antibody Complex, Binding Sites, Crystallography, X-Ray, Epitopes, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Immunoglobulin Fab Fragments (chemistry), Immunoglobulin Fab Fragments (immunology), Immunoglobulin Fab Fragments (metabolism), Influenza A Virus, H2N2 Subtype (immunology), Molecular Sequence Data, Mutation, Protein Conformation, Tryptophan (immunology), Tryptophan (metabolism), Tyrosine (metabolism).
- MESH :
- chemical , chemistry : Antibodies, Neutralizing, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments.
- chemical , genetics : Antibodies, Viral.
- chemical , immunology : Antibodies, Neutralizing, Antibodies, Viral, Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments, Tryptophan.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Immunoglobulin Fab Fragments, Tryptophan, Tyrosine.
- immunology : Influenza A Virus, H2N2 Subtype.
- Amino Acid Motifs, Amino Acid Sequence, Antigen-Antibody Complex, Binding Sites, Crystallography, X-Ray, Epitopes, Humans, Molecular Sequence Data, Mutation, Protein Conformation.
Abstract
Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral entry blockers has not been successful, suggesting that sialic acid may not be an ideal scaffold to obtain broad and potent HA inhibitors. Here we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two VH1-69 antibodies or a tyrosine from HCDR3 in the other antibody. This remarkably conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.
Url:
DOI: 10.1038/nsmb.2500
PubMed: 23396351
PubMed Central: 3594569
Affiliations:
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PMC:3594569Le document en format XML
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Wilson</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology, The Scripps Research Institute, La Jolla, California</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="A5">Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><series><title level="j">Nature structural & molecular biology</title><idno type="ISSN">1545-9993</idno><idno type="eISSN">1545-9985</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Antibodies, Neutralizing (chemistry)</term><term>Antibodies, Neutralizing (immunology)</term><term>Antibodies, Viral (genetics)</term><term>Antibodies, Viral (immunology)</term><term>Antigen-Antibody Complex</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Epitopes</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (immunology)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term><term>Humans</term><term>Immunoglobulin Fab Fragments (chemistry)</term><term>Immunoglobulin Fab Fragments (immunology)</term><term>Immunoglobulin Fab Fragments (metabolism)</term><term>Influenza A Virus, H2N2 Subtype (immunology)</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Conformation</term><term>Tryptophan (immunology)</term><term>Tryptophan (metabolism)</term><term>Tyrosine (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps antiviraux (génétique)</term><term>Anticorps antiviraux (immunologie)</term><term>Anticorps neutralisants ()</term><term>Anticorps neutralisants (immunologie)</term><term>Complexe antigène-anticorps</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Fragments Fab d'immunoglobuline ()</term><term>Fragments Fab d'immunoglobuline (immunologie)</term><term>Fragments Fab d'immunoglobuline (métabolisme)</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Humains</term><term>Motifs d'acides aminés</term><term>Mutation</term><term>Sites de fixation</term><term>Sous-type H2N2 du virus de la grippe A (immunologie)</term><term>Séquence d'acides aminés</term><term>Tryptophane (immunologie)</term><term>Tryptophane (métabolisme)</term><term>Tyrosine (métabolisme)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Neutralizing</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Neutralizing</term><term>Antibodies, Viral</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term><term>Tryptophan</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Immunoglobulin Fab Fragments</term><term>Tryptophan</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Anticorps antiviraux</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps neutralisants</term><term>Fragments Fab d'immunoglobuline</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Tryptophane</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A Virus, H2N2 Subtype</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments Fab d'immunoglobuline</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Tryptophane</term><term>Tyrosine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Antigen-Antibody Complex</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Epitopes</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anticorps neutralisants</term><term>Complexe antigène-anticorps</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Fragments Fab d'immunoglobuline</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Humains</term><term>Motifs d'acides aminés</term><term>Mutation</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Influenza virus hemagglutinin (HA) mediates receptor binding and viral entry during influenza infection. The development of receptor analogs as viral entry blockers has not been successful, suggesting that sialic acid may not be an ideal scaffold to obtain broad and potent HA inhibitors. Here we report crystal structures of Fab fragments from three human antibodies that neutralize the 1957 pandemic H2N2 influenza virus in complex with H2 HA. All three antibodies use an aromatic residue to plug a conserved cavity in the HA receptor-binding site. Each antibody interacts with the absolutely conserved HA1 Trp153 at the cavity base through π-π stacking with the signature Phe54 of two V<sub>H</sub>1-69 antibodies or a tyrosine from HCDR3 in the other antibody. This remarkably conserved interaction can be used as a starting point to design inhibitors targeting this conserved hydrophobic pocket in influenza viruses.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Gilbert, Sc" uniqKey="Gilbert S">SC Gilbert</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ekiert, Dc" uniqKey="Ekiert D">DC Ekiert</name></author><author><name sortKey="Wilson, Ia" uniqKey="Wilson I">IA Wilson</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Du, J" uniqKey="Du J">J Du</name></author><author><name sortKey="Cross, Ta" uniqKey="Cross T">TA Cross</name></author><author><name sortKey="Zhou, Hx" uniqKey="Zhou H">HX Zhou</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Skehel, J" uniqKey="Skehel J">J Skehel</name></author><author><name sortKey="Wiley, D" uniqKey="Wiley D">D 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Wilson</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li><li>Tennessee</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Xu, Rui" sort="Xu, Rui" uniqKey="Xu R" first="Rui" last="Xu">Rui Xu</name></region><name sortKey="Crowe, James E" sort="Crowe, James E" uniqKey="Crowe J" first="James E." last="Crowe">James E. Crowe</name><name sortKey="Crowe, James E" sort="Crowe, James E" uniqKey="Crowe J" first="James E." last="Crowe">James E. Crowe</name><name sortKey="Krause, Jens C" sort="Krause, Jens C" uniqKey="Krause J" first="Jens C." last="Krause">Jens C. Krause</name><name sortKey="Mcbride, Ryan" sort="Mcbride, Ryan" uniqKey="Mcbride R" first="Ryan" last="Mcbride">Ryan Mcbride</name><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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