Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957.
Identifieur interne : 000513 ( Main/Exploration ); précédent : 000512; suivant : 000514Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957.
Auteurs : Junfeng Liu [Royaume-Uni] ; David J. Stevens ; Lesley F. Haire ; Philip A. Walker ; Peter J. Coombs ; Rupert J. Russell ; Steven J. Gamblin ; John J. SkehelSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Asie (épidémiologie), Cristallographie aux rayons X (MeSH), Espagne (épidémiologie), Glycoprotéine hémagglutinine du virus influenza (composition chimique), Glycoprotéine hémagglutinine du virus influenza (génétique), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Grippe chez les oiseaux (virologie), Grippe humaine (virologie), Grippe humaine (épidémiologie), Hong Kong (épidémiologie), Humains (MeSH), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Mutation (MeSH), Oiseaux (MeSH), Récepteurs viraux (composition chimique), Récepteurs viraux (métabolisme), Sites de fixation (génétique), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Virus de la grippe A (génétique), Virus de la grippe A (métabolisme), Épidémies de maladies (MeSH).
- MESH :
- composition chimique : Glycoprotéine hémagglutinine du virus influenza, Récepteurs viraux.
- génétique : Glycoprotéine hémagglutinine du virus influenza, Sites de fixation, Virus de la grippe A.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Récepteurs viraux, Virus de la grippe A.
- virologie : Grippe chez les oiseaux, Grippe humaine.
- épidémiologie : Asie, Espagne, Grippe humaine, Hong Kong.
- Animaux, Cristallographie aux rayons X, Humains, Liaison aux protéines, Modèles moléculaires, Mutation, Oiseaux, Structure secondaire des protéines, Structure tertiaire des protéines, Épidémies de maladies.
- Wicri :
English descriptors
- KwdEn :
- Animals (MeSH), Asia (epidemiology), Binding Sites (genetics), Birds (MeSH), Crystallography, X-Ray (MeSH), Disease Outbreaks (MeSH), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Hong Kong (epidemiology), Humans (MeSH), Influenza A virus (genetics), Influenza A virus (metabolism), Influenza in Birds (virology), Influenza, Human (epidemiology), Influenza, Human (virology), Models, Molecular (MeSH), Mutation (MeSH), Protein Binding (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Receptors, Virus (chemistry), Receptors, Virus (metabolism), Spain (epidemiology).
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus, Receptors, Virus.
- geographic , epidemiology : Asia, Hong Kong, Spain.
- epidemiology : Influenza, Human.
- genetics : Binding Sites, Hemagglutinin Glycoproteins, Influenza Virus, Influenza A virus.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Influenza A virus, Receptors, Virus.
- virology : Influenza in Birds, Influenza, Human.
- Animals, Birds, Crystallography, X-Ray, Disease Outbreaks, Humans, Models, Molecular, Mutation, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
The viruses that caused the three influenza pandemics of the twentieth century in 1918, 1957, and 1968 had distinct hemagglutinin receptor binding glycoproteins that had evolved the capacity to recognize human cell receptors. We have determined the structure of the H2 hemagglutinin from the second pandemic, the "Asian Influenza" of 1957. We compare it with the 1918 "Spanish Influenza" hemagglutinin, H1, and the 1968 "Hong Kong Influenza" hemagglutinin, H3, and show that despite its close overall structural similarity to H1, and its more distant relationship to H3, the H2 receptor binding site is closely related to that of H3 hemagglutinin. By analyzing hemagglutinins of potential H2 avian precursors of the pandemic virus, we show that the human receptor can be bound by avian hemagglutinins that lack the human-specific mutations of H2 and H3 pandemic viruses, Gln-226Leu, and Gly-228Ser. We show how Gln-226 in the avian H2 receptor binding site, together with Asn-186, form hydrogen bond networks through bound water molecules to mediate binding to human receptor. We show that the human receptor adopts a very similar conformation in both human and avian hemagglutinin-receptor complexes. We also show that Leu-226 in the receptor binding site of human virus hemagglutinins creates a hydrophobic environment near the Sia-1-Gal-2 glycosidic linkage that favors binding of the human receptor and is unfavorable for avian receptor binding. We consider the significance for the development of pandemics, of the existence of avian viruses that can bind to both avian and human receptors.
DOI: 10.1073/pnas.0906849106
PubMed: 19805083
PubMed Central: PMC2761367
Affiliations:
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(epidemiology)</term><term>Influenza, Human (virology)</term><term>Models, Molecular (MeSH)</term><term>Mutation (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Spain (epidemiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Asie (épidémiologie)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Espagne (épidémiologie)</term><term>Glycoprotéine hémagglutinine du virus influenza (composition chimique)</term><term>Glycoprotéine hémagglutinine du virus influenza (génétique)</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Grippe chez les oiseaux (virologie)</term><term>Grippe humaine (virologie)</term><term>Grippe humaine (épidémiologie)</term><term>Hong Kong (épidémiologie)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutation (MeSH)</term><term>Oiseaux (MeSH)</term><term>Récepteurs viraux (composition chimique)</term><term>Récepteurs viraux (métabolisme)</term><term>Sites de fixation (génétique)</term><term>Structure secondaire des protéines (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Virus de la grippe A (génétique)</term><term>Virus de la grippe A (métabolisme)</term><term>Épidémies de maladies (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="geographic" qualifier="epidemiology" xml:lang="en"><term>Asia</term><term>Hong Kong</term><term>Spain</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Sites de fixation</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza A virus</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Récepteurs viraux</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Grippe chez les oiseaux</term><term>Grippe humaine</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Influenza in Birds</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Asie</term><term>Espagne</term><term>Grippe humaine</term><term>Hong Kong</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Birds</term><term>Crystallography, X-Ray</term><term>Disease Outbreaks</term><term>Humans</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cristallographie aux rayons X</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Mutation</term><term>Oiseaux</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Épidémies de maladies</term></keywords><keywords scheme="Wicri" type="geographic" xml:lang="fr"><term>Hong Kong</term><term>Espagne</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The viruses that caused the three influenza pandemics of the twentieth century in 1918, 1957, and 1968 had distinct hemagglutinin receptor binding glycoproteins that had evolved the capacity to recognize human cell receptors. We have determined the structure of the H2 hemagglutinin from the second pandemic, the "Asian Influenza" of 1957. We compare it with the 1918 "Spanish Influenza" hemagglutinin, H1, and the 1968 "Hong Kong Influenza" hemagglutinin, H3, and show that despite its close overall structural similarity to H1, and its more distant relationship to H3, the H2 receptor binding site is closely related to that of H3 hemagglutinin. By analyzing hemagglutinins of potential H2 avian precursors of the pandemic virus, we show that the human receptor can be bound by avian hemagglutinins that lack the human-specific mutations of H2 and H3 pandemic viruses, Gln-226Leu, and Gly-228Ser. We show how Gln-226 in the avian H2 receptor binding site, together with Asn-186, form hydrogen bond networks through bound water molecules to mediate binding to human receptor. We show that the human receptor adopts a very similar conformation in both human and avian hemagglutinin-receptor complexes. We also show that Leu-226 in the receptor binding site of human virus hemagglutinins creates a hydrophobic environment near the Sia-1-Gal-2 glycosidic linkage that favors binding of the human receptor and is unfavorable for avian receptor binding. We consider the significance for the development of pandemics, of the existence of avian viruses that can bind to both avian and human receptors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19805083</PMID><DateCompleted><Year>2010</Year><Month>01</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>106</Volume><Issue>40</Issue><PubDate><Year>2009</Year><Month>Oct</Month><Day>06</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957.</ArticleTitle><Pagination><MedlinePgn>17175-80</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.0906849106</ELocationID><Abstract><AbstractText>The viruses that caused the three influenza pandemics of the twentieth century in 1918, 1957, and 1968 had distinct hemagglutinin receptor binding glycoproteins that had evolved the capacity to recognize human cell receptors. We have determined the structure of the H2 hemagglutinin from the second pandemic, the "Asian Influenza" of 1957. We compare it with the 1918 "Spanish Influenza" hemagglutinin, H1, and the 1968 "Hong Kong Influenza" hemagglutinin, H3, and show that despite its close overall structural similarity to H1, and its more distant relationship to H3, the H2 receptor binding site is closely related to that of H3 hemagglutinin. By analyzing hemagglutinins of potential H2 avian precursors of the pandemic virus, we show that the human receptor can be bound by avian hemagglutinins that lack the human-specific mutations of H2 and H3 pandemic viruses, Gln-226Leu, and Gly-228Ser. We show how Gln-226 in the avian H2 receptor binding site, together with Asn-186, form hydrogen bond networks through bound water molecules to mediate binding to human receptor. We show that the human receptor adopts a very similar conformation in both human and avian hemagglutinin-receptor complexes. We also show that Leu-226 in the receptor binding site of human virus hemagglutinins creates a hydrophobic environment near the Sia-1-Gal-2 glycosidic linkage that favors binding of the human receptor and is unfavorable for avian receptor binding. We consider the significance for the development of pandemics, of the existence of avian viruses that can bind to both avian and human receptors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Junfeng</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stevens</LastName><ForeName>David J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Haire</LastName><ForeName>Lesley F</ForeName><Initials>LF</Initials></Author><Author ValidYN="Y"><LastName>Walker</LastName><ForeName>Philip A</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Coombs</LastName><ForeName>Peter J</ForeName><Initials>PJ</Initials></Author><Author ValidYN="Y"><LastName>Russell</LastName><ForeName>Rupert J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Gamblin</LastName><ForeName>Steven J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Skehel</LastName><ForeName>John J</ForeName><Initials>JJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MC_U117584222</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>09</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C109963">hemagglutinin, avian influenza A virus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001208" MajorTopicYN="N" Type="Geographic">Asia</DescriptorName><QualifierName UI="Q000453" MajorTopicYN="N">epidemiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001717" MajorTopicYN="N">Birds</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004196" MajorTopicYN="N">Disease Outbreaks</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019267" MajorTopicYN="N">Hemagglutinin Glycoproteins, Influenza Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006723" MajorTopicYN="N" Type="Geographic">Hong Kong</DescriptorName><QualifierName UI="Q000453" MajorTopicYN="N">epidemiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005585" MajorTopicYN="N">Influenza in Birds</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName><QualifierName UI="Q000453" MajorTopicYN="N">epidemiology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="Y">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013030" MajorTopicYN="N" Type="Geographic">Spain</DescriptorName><QualifierName UI="Q000453" MajorTopicYN="N">epidemiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>10</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">10567648</ArticleId></ArticleIdList></Reference><Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation><ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1979 Mar 25;254(6):2120-4</Citation><ArticleIdList><ArticleId IdType="pubmed">422571</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1989 Oct 17;28(21):8388-96</Citation><ArticleIdList><ArticleId IdType="pubmed">2605190</ArticleId></ArticleIdList></Reference><Reference><Citation>Bull World Health Organ. 1980;58(4):585-91</Citation><ArticleIdList><ArticleId IdType="pubmed">6969132</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17033-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15563589</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2003 May 10;309(2):209-18</Citation><ArticleIdList><ArticleId IdType="pubmed">12758169</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2004 Aug 1;325(2):287-96</Citation><ArticleIdList><ArticleId IdType="pubmed">15246268</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Soc Exp Biol Med. 1957 Jul;95(3):609-16</Citation><ArticleIdList><ArticleId IdType="pubmed">13453522</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1989 Nov;63(11):4603-8</Citation><ArticleIdList><ArticleId IdType="pubmed">2795713</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2006 May 23;103(21):8060-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16690741</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1998 Oct 30;95(3):409-17</Citation><ArticleIdList><ArticleId IdType="pubmed">9814710</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2000 Sep;74(18):8502-12</Citation><ArticleIdList><ArticleId IdType="pubmed">10954551</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2005 Apr 10;334(2):276-83</Citation><ArticleIdList><ArticleId IdType="pubmed">15780877</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1984 Aug;51(2):567-9</Citation><ArticleIdList><ArticleId IdType="pubmed">6748165</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1978 Jun 1;87(1):13-20</Citation><ArticleIdList><ArticleId IdType="pubmed">664248</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 1958 Apr 19;1(7025):810-4</Citation><ArticleIdList><ArticleId IdType="pubmed">13526279</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1994 Nov 15;205(1):17-23</Citation><ArticleIdList><ArticleId IdType="pubmed">7975212</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1983 Jun;127(2):361-73</Citation><ArticleIdList><ArticleId IdType="pubmed">6868370</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4620-4</Citation><ArticleIdList><ArticleId IdType="pubmed">15070767</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1981 Jul 2;292(5818):72-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7278968</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 1995 Oct 16;164(1):49-53</Citation><ArticleIdList><ArticleId IdType="pubmed">7590320</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54</Citation><ArticleIdList><ArticleId IdType="pubmed">12393927</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Biochem. 2000;69:531-69</Citation><ArticleIdList><ArticleId IdType="pubmed">10966468</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1988 Jun 2;333(6172):426-31</Citation><ArticleIdList><ArticleId IdType="pubmed">3374584</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1997 Jun 23;233(1):224-34</Citation><ArticleIdList><ArticleId IdType="pubmed">9201232</ArticleId></ArticleIdList></Reference><Reference><Citation>J Hyg Epidemiol Microbiol Immunol. 1958;2(1):1-8</Citation><ArticleIdList><ArticleId IdType="pubmed">13598889</ArticleId></ArticleIdList></Reference><Reference><Citation>Emerg Infect Dis. 2006 Jan;12(1):34-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16494714</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3</Citation><ArticleIdList><ArticleId IdType="pubmed">15299374</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11181-6</Citation><ArticleIdList><ArticleId IdType="pubmed">11562490</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation><ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2004 Mar 19;303(5665):1838-42</Citation><ArticleIdList><ArticleId IdType="pubmed">14764886</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Med. 1960 Oct 31;112(5):895-920</Citation><ArticleIdList><ArticleId IdType="pubmed">19867182</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1651-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9990079</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 1993 Aug;29(2):155-65</Citation><ArticleIdList><ArticleId IdType="pubmed">8212857</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1978 Feb;84(2):268-78</Citation><ArticleIdList><ArticleId IdType="pubmed">23604</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1981 Jan 29;289(5796):366-73</Citation><ArticleIdList><ArticleId IdType="pubmed">7464906</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1993 Jun;194(2):781-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7684877</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 1957 Oct 19;273(6999):791-6</Citation><ArticleIdList><ArticleId IdType="pubmed">13476727</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Histochem Suppl. 1990;40:35-8</Citation><ArticleIdList><ArticleId IdType="pubmed">2091044</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Coombs, Peter J" sort="Coombs, Peter J" uniqKey="Coombs P" first="Peter J" last="Coombs">Peter J. Coombs</name><name sortKey="Gamblin, Steven J" sort="Gamblin, Steven J" uniqKey="Gamblin S" first="Steven J" last="Gamblin">Steven J. Gamblin</name><name sortKey="Haire, Lesley F" sort="Haire, Lesley F" uniqKey="Haire L" first="Lesley F" last="Haire">Lesley F. Haire</name><name sortKey="Russell, Rupert J" sort="Russell, Rupert J" uniqKey="Russell R" first="Rupert J" last="Russell">Rupert J. Russell</name><name sortKey="Skehel, John J" sort="Skehel, John J" uniqKey="Skehel J" first="John J" last="Skehel">John J. Skehel</name><name sortKey="Stevens, David J" sort="Stevens, David J" uniqKey="Stevens D" first="David J" last="Stevens">David J. Stevens</name><name sortKey="Walker, Philip A" sort="Walker, Philip A" uniqKey="Walker P" first="Philip A" last="Walker">Philip A. Walker</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Liu, Junfeng" sort="Liu, Junfeng" uniqKey="Liu J" first="Junfeng" last="Liu">Junfeng Liu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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