Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase
Identifieur interne : 002555 ( Main/Merge ); précédent : 002554; suivant : 002556Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase
Auteurs : G. M. Air [États-Unis] ; M. C. Els [États-Unis] ; L. E. Brown [Australie] ; W. G. Laver [Australie] ; R. G. Webster [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1985.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux, Conformation des protéines, Embryon de poulet, Gènes, Gènes viraux, Modèles moléculaires, Sialidase (génétique), Sialidase (immunologie), Séquence d'acides aminés, Séquence nucléotidique, Variation génétique, Virus de la grippe A (enzymologie), Virus de la grippe A (génétique), Épitopes (analyse).
- MESH :
- analyse : Épitopes.
- enzymologie : Virus de la grippe A.
- génétique : Sialidase, Virus de la grippe A.
- immunologie : Sialidase.
- Animaux, Anticorps monoclonaux, Conformation des protéines, Embryon de poulet, Gènes, Gènes viraux, Modèles moléculaires, Séquence d'acides aminés, Séquence nucléotidique, Variation génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Chick Embryo, Epitopes (analysis), Genes, Genes, Viral, Genetic Variation, Influenza A virus (enzymology), Influenza A virus (genetics), Models, Molecular, Neuraminidase (genetics), Neuraminidase (immunology), Protein Conformation.
- MESH :
- chemical , analysis : Epitopes.
- chemical , genetics : Neuraminidase.
- chemical , immunology : Neuraminidase.
- enzymology : Influenza A virus.
- genetics : Influenza A virus.
- Teeft :
- Academic press, Active site pocket, Amino, Amino Acid Sequence, Amino acid, Amino acid sequence changes, Anhydride, Animals, Antibodies, Monoclonal, Antibody, Antibody binding, Antigenic, Antigenic analysis, Antigenic drift, Antigenic properties, Antigenic sites, Antigenic structure, Antigenic variants, Assay, Base Sequence, Chemical modification, Chick Embryo, Competition assays, Dideoxy method, Elisa assays, Enzyme activity, Fdnb, Genes, Genes, Viral, Genetic Variation, Good correlation, Hemagglutinin, Hong kong, Influenza, Influenza virus, Influenza virus hemagglutinin, Influenza virus neuraminidase, Influenza viruses, Laver, Lysine, Mdck cells, Models, Molecular, Monoclonal, Monoclonal antibodies, Monoclonal variants, Neuraminidase, Neuraminidase genes, Nucleotide, Parental virus, Peptide, Peptide analysis, Protein Conformation, Reassortant virus, Same residues, Sequence analysis, Sequence change, Sequence changes, Sequencing, Several variants, Succinic anhydride, Threedimensional structure, Tryptic peptides, Varghese, Variant, Variant viruses, Virology, Virology laver, Virus, Virus neuraminidase, Virus particles, Virus strains, Webster.
Abstract
Abstract: Sequence analysis of the neuraminidase (NA) genes of influenza virus X-7(F1) and of 12 variants selected with monoclonal antibodies has been used to define in physical terms the antigenic structure of this NA, which was operationally established by R. G. Webster, L. E. Brown, and W. G. Laver (1984, Virology 135, 30–42). X-7(F1) is a reassortant virus containing the NA of the early Asian (H2N2) isolate A/RI/5+/57, and the results of antigenic and sequence analysis of X-7(F1) and of variants selected with monoclonal antibodies have been combined with a similar analysis of the A/Tokyo/3/67 NA (H2N2, M. R. Lentz, G. M. Air, W. G. Laver, and R. G. Webster (1984), Virology 135, 257–265) to obtain a model of antibody binding to N2 NAs. The selection process was biased, however, since only those monoclonal antibodies which inhibited NA activity could be used to select variants. Most of the changes in the variants selected with monoclonal antibodies occur in those parts of the polypeptide chain which encircle the enzyme active site pocket in the three-dimensional structure (P. M. Colman, J. N. Varghese, and W. G. Laver (1983), Nature (London) 303, 41–44). The results suggest that in general the antibody binds to a site on the NA which includes those amino acid side chains which are altered in monoclonal variants. There are, however, several aspects of the antigen-antibody interaction which are not easily explained, and which will probably only be fully elucidated by X-ray crystallographic analysis of NA-antibody complexes.
Url:
DOI: 10.1016/0042-6822(85)90157-6
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Webster</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>St. Jude Childrens Research Hospital, Memphis, Tennessee, 38101</wicri:regionArea><wicri:noRegion>38101</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1985">1985</date><biblScope unit="volume">145</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="237">237</biblScope><biblScope unit="page" to="248">248</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibodies, Monoclonal</term><term>Base Sequence</term><term>Chick Embryo</term><term>Epitopes (analysis)</term><term>Genes</term><term>Genes, Viral</term><term>Genetic Variation</term><term>Influenza A virus (enzymology)</term><term>Influenza A virus (genetics)</term><term>Models, Molecular</term><term>Neuraminidase (genetics)</term><term>Neuraminidase (immunology)</term><term>Protein Conformation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Embryon de poulet</term><term>Gènes</term><term>Gènes viraux</term><term>Modèles moléculaires</term><term>Sialidase (génétique)</term><term>Sialidase (immunologie)</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Variation génétique</term><term>Virus de la grippe A (enzymologie)</term><term>Virus de la grippe A (génétique)</term><term>Épitopes (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Sialidase</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Active site pocket</term><term>Amino</term><term>Amino Acid Sequence</term><term>Amino acid</term><term>Amino acid sequence changes</term><term>Anhydride</term><term>Animals</term><term>Antibodies, Monoclonal</term><term>Antibody</term><term>Antibody binding</term><term>Antigenic</term><term>Antigenic analysis</term><term>Antigenic drift</term><term>Antigenic properties</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Antigenic variants</term><term>Assay</term><term>Base Sequence</term><term>Chemical modification</term><term>Chick Embryo</term><term>Competition assays</term><term>Dideoxy method</term><term>Elisa assays</term><term>Enzyme activity</term><term>Fdnb</term><term>Genes</term><term>Genes, Viral</term><term>Genetic Variation</term><term>Good correlation</term><term>Hemagglutinin</term><term>Hong kong</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Laver</term><term>Lysine</term><term>Mdck cells</term><term>Models, Molecular</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal variants</term><term>Neuraminidase</term><term>Neuraminidase genes</term><term>Nucleotide</term><term>Parental virus</term><term>Peptide</term><term>Peptide analysis</term><term>Protein Conformation</term><term>Reassortant virus</term><term>Same residues</term><term>Sequence analysis</term><term>Sequence change</term><term>Sequence changes</term><term>Sequencing</term><term>Several variants</term><term>Succinic anhydride</term><term>Threedimensional structure</term><term>Tryptic peptides</term><term>Varghese</term><term>Variant</term><term>Variant viruses</term><term>Virology</term><term>Virology laver</term><term>Virus</term><term>Virus neuraminidase</term><term>Virus particles</term><term>Virus strains</term><term>Webster</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Embryon de poulet</term><term>Gènes</term><term>Gènes viraux</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Variation génétique</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Sequence analysis of the neuraminidase (NA) genes of influenza virus X-7(F1) and of 12 variants selected with monoclonal antibodies has been used to define in physical terms the antigenic structure of this NA, which was operationally established by R. G. Webster, L. E. Brown, and W. G. Laver (1984, Virology 135, 30–42). X-7(F1) is a reassortant virus containing the NA of the early Asian (H2N2) isolate A/RI/5+/57, and the results of antigenic and sequence analysis of X-7(F1) and of variants selected with monoclonal antibodies have been combined with a similar analysis of the A/Tokyo/3/67 NA (H2N2, M. R. Lentz, G. M. Air, W. G. Laver, and R. G. Webster (1984), Virology 135, 257–265) to obtain a model of antibody binding to N2 NAs. The selection process was biased, however, since only those monoclonal antibodies which inhibited NA activity could be used to select variants. Most of the changes in the variants selected with monoclonal antibodies occur in those parts of the polypeptide chain which encircle the enzyme active site pocket in the three-dimensional structure (P. M. Colman, J. N. Varghese, and W. G. Laver (1983), Nature (London) 303, 41–44). The results suggest that in general the antibody binds to a site on the NA which includes those amino acid side chains which are altered in monoclonal variants. There are, however, several aspects of the antigen-antibody interaction which are not easily explained, and which will probably only be fully elucidated by X-ray crystallographic analysis of NA-antibody complexes.</div></front></TEI><double doi="10.1016/0042-6822(85)90157-6"><ISTEX><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase</title><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name></author><author><name sortKey="Els, M C" sort="Els, M C" uniqKey="Els M" first="M. C." last="Els">M. C. Els</name></author><author><name sortKey="Brown, L E" sort="Brown, L E" uniqKey="Brown L" first="L. E." last="Brown">L. E. Brown</name></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:706CCB0A4EF7296660D54B9BBA97DB4003EDE412</idno><date when="1985" year="1985">1985</date><idno type="doi">10.1016/0042-6822(85)90157-6</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-FFGDZ4B0-M/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000178</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000178</idno><idno type="wicri:Area/Istex/Curation">000178</idno><idno type="wicri:Area/Istex/Checkpoint">001116</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001116</idno><idno type="wicri:doubleKey">0042-6822:1985:Air G:location:of:antigenic</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase</title><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294</wicri:regionArea><wicri:noRegion>Alabama 35294</wicri:noRegion></affiliation></author><author><name sortKey="Els, M C" sort="Els, M C" uniqKey="Els M" first="M. C." last="Els">M. C. Els</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294</wicri:regionArea><wicri:noRegion>Alabama 35294</wicri:noRegion></affiliation></author><author><name sortKey="Brown, L E" sort="Brown, L E" uniqKey="Brown L" first="L. E." last="Brown">L. E. Brown</name><affiliation wicri:level="4"><country xml:lang="fr">Australie</country><wicri:regionArea>Microbiology Department, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>John Curtin School of Medical Research, Canberra City, 2601</wicri:regionArea><wicri:noRegion>2601</wicri:noRegion></affiliation></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>St. Jude Childrens Research Hospital, Memphis, Tennessee, 38101</wicri:regionArea><wicri:noRegion>38101</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1985">1985</date><biblScope unit="volume">145</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="237">237</biblScope><biblScope unit="page" to="248">248</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Active site pocket</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence changes</term><term>Anhydride</term><term>Antibody</term><term>Antibody binding</term><term>Antigenic</term><term>Antigenic analysis</term><term>Antigenic drift</term><term>Antigenic properties</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Antigenic variants</term><term>Assay</term><term>Chemical modification</term><term>Competition assays</term><term>Dideoxy method</term><term>Elisa assays</term><term>Enzyme activity</term><term>Fdnb</term><term>Good correlation</term><term>Hemagglutinin</term><term>Hong kong</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Laver</term><term>Lysine</term><term>Mdck cells</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal variants</term><term>Neuraminidase</term><term>Neuraminidase genes</term><term>Nucleotide</term><term>Parental virus</term><term>Peptide</term><term>Peptide analysis</term><term>Reassortant virus</term><term>Same residues</term><term>Sequence analysis</term><term>Sequence change</term><term>Sequence changes</term><term>Sequencing</term><term>Several variants</term><term>Succinic anhydride</term><term>Threedimensional structure</term><term>Tryptic peptides</term><term>Varghese</term><term>Variant</term><term>Variant viruses</term><term>Virology</term><term>Virology laver</term><term>Virus</term><term>Virus neuraminidase</term><term>Virus particles</term><term>Virus strains</term><term>Webster</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Sequence analysis of the neuraminidase (NA) genes of influenza virus X-7(F1) and of 12 variants selected with monoclonal antibodies has been used to define in physical terms the antigenic structure of this NA, which was operationally established by R. G. Webster, L. E. Brown, and W. G. Laver (1984, Virology 135, 30–42). X-7(F1) is a reassortant virus containing the NA of the early Asian (H2N2) isolate A/RI/5+/57, and the results of antigenic and sequence analysis of X-7(F1) and of variants selected with monoclonal antibodies have been combined with a similar analysis of the A/Tokyo/3/67 NA (H2N2, M. R. Lentz, G. M. Air, W. G. Laver, and R. G. Webster (1984), Virology 135, 257–265) to obtain a model of antibody binding to N2 NAs. The selection process was biased, however, since only those monoclonal antibodies which inhibited NA activity could be used to select variants. Most of the changes in the variants selected with monoclonal antibodies occur in those parts of the polypeptide chain which encircle the enzyme active site pocket in the three-dimensional structure (P. M. Colman, J. N. Varghese, and W. G. Laver (1983), Nature (London) 303, 41–44). The results suggest that in general the antibody binds to a site on the NA which includes those amino acid side chains which are altered in monoclonal variants. There are, however, several aspects of the antigen-antibody interaction which are not easily explained, and which will probably only be fully elucidated by X-ray crystallographic analysis of NA-antibody complexes.</div></front></TEI></ISTEX><PubMed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase.</title><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G M" last="Air">G M Air</name></author><author><name sortKey="Els, M C" sort="Els, M C" uniqKey="Els M" first="M C" last="Els">M C Els</name></author><author><name sortKey="Brown, L E" sort="Brown, L E" uniqKey="Brown L" first="L E" last="Brown">L E Brown</name></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W G" last="Laver">W G Laver</name></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R G" last="Webster">R G Webster</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1985">1985</date><idno type="RBID">pubmed:2411049</idno><idno type="pmid">2411049</idno><idno type="doi">10.1016/0042-6822(85)90157-6</idno><idno type="wicri:Area/PubMed/Corpus">000504</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000504</idno><idno type="wicri:Area/PubMed/Curation">000504</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000504</idno><idno type="wicri:Area/PubMed/Checkpoint">000446</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000446</idno><idno type="wicri:Area/Ncbi/Merge">000969</idno><idno type="wicri:Area/Ncbi/Curation">000969</idno><idno type="wicri:Area/Ncbi/Checkpoint">000969</idno><idno type="wicri:doubleKey">0042-6822:1985:Air G:location:of:antigenic</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase.</title><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G M" last="Air">G M Air</name></author><author><name sortKey="Els, M C" sort="Els, M C" uniqKey="Els M" first="M C" last="Els">M C Els</name></author><author><name sortKey="Brown, L E" sort="Brown, L E" uniqKey="Brown L" first="L E" last="Brown">L E Brown</name></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W G" last="Laver">W G Laver</name></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R G" last="Webster">R G Webster</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><imprint><date when="1985" type="published">1985</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibodies, Monoclonal</term><term>Base Sequence</term><term>Chick Embryo</term><term>Epitopes (analysis)</term><term>Genes</term><term>Genes, Viral</term><term>Genetic Variation</term><term>Influenza A virus (enzymology)</term><term>Influenza A virus (genetics)</term><term>Models, Molecular</term><term>Neuraminidase (genetics)</term><term>Neuraminidase (immunology)</term><term>Protein Conformation</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Embryon de poulet</term><term>Gènes</term><term>Gènes viraux</term><term>Modèles moléculaires</term><term>Sialidase (génétique)</term><term>Sialidase (immunologie)</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Variation génétique</term><term>Virus de la grippe A (enzymologie)</term><term>Virus de la grippe A (génétique)</term><term>Épitopes (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Sialidase</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Chick Embryo</term><term>Genes</term><term>Genes, Viral</term><term>Genetic Variation</term><term>Models, Molecular</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux</term><term>Conformation des protéines</term><term>Embryon de poulet</term><term>Gènes</term><term>Gènes viraux</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Variation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sequence analysis of the neuraminidase (NA) genes of influenza virus X-7(F1) and of 12 variants selected with monoclonal antibodies has been used to define in physical terms the antigenic structure of this NA, which was operationally established by R. G. Webster, L. E. Brown, and W. G. Laver (1984, Virology 135, 30-42). X-7(F1) is a reassortant virus containing the NA of the early Asian (H2N2) isolate A/RI/5+/57, and the results of antigenic and sequence analysis of X-7(F1) and of variants selected with monoclonal antibodies have been combined with a similar analysis of the A/Tokyo/3/67 NA (H2N2, M. R. Lentz, G. M. Air, W. G. Laver, and R. G. Webster (1984), Virology 135, 257-265) to obtain a model of antibody binding to N2 NAs. The selection process was biased, however, since only those monoclonal antibodies which inhibited NA activity could be used to select variants. Most of the changes in the variants selected with monoclonal antibodies occur in those parts of the polypeptide chain which encircle the enzyme active site pocket in the three-dimensional structure (P. M. Colman, J. N. Varghese, and W. G. Laver (1983), Nature (London) 303, 41-44). The results suggest that in general the antibody binds to a site on the NA which includes those amino acid side chains which are altered in monoclonal variants. There are, however, several aspects of the antigen-antibody interaction which are not easily explained, and which will probably only be fully elucidated by X-ray crystallographic analysis of NA-antibody complexes.</div></front></TEI></PubMed></double></record>Pour manipuler ce document sous Unix (Dilib)
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