Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
Identifieur interne : 001F46 ( Main/Exploration ); précédent : 001F45; suivant : 001F47Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
Auteurs : M. N. Matrosovich [Russie] ; A. S. Gambaryan [Russie] ; M. P. Chumakov [Russie]Source :
- Virology [ 0042-6822 ] ; 1992.
Descripteurs français
- KwdFr :
- Acides sialiques (), Acides sialiques (métabolisme), Hémagglutinines virales (métabolisme), Hémagglutinines virales (ultrastructure), Liaison aux protéines, Modèles moléculaires, Orthomyxoviridae (métabolisme), Relation structure-activité, Récepteurs viraux (), Récepteurs viraux (métabolisme), Sialidase (pharmacologie), Séquence glucidique, alpha-Macroglobulines.
- MESH :
- métabolisme : Acides sialiques, Hémagglutinines virales, Orthomyxoviridae, Récepteurs viraux.
- pharmacologie : Sialidase.
- ultrastructure : Hémagglutinines virales.
- Acides sialiques, Liaison aux protéines, Modèles moléculaires, Relation structure-activité, Récepteurs viraux, Séquence glucidique, alpha-Macroglobulines.
English descriptors
- KwdEn :
- Carbohydrate Sequence, Hemagglutinins, Viral (metabolism), Hemagglutinins, Viral (ultrastructure), Models, Molecular, Neuraminidase (pharmacology), Orthomyxoviridae (metabolism), Protein Binding, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Sialic Acids (chemistry), Sialic Acids (metabolism), Structure-Activity Relationship, alpha-Macroglobulins.
- MESH :
- chemical , chemistry : Receptors, Virus, Sialic Acids.
- chemical , metabolism : Hemagglutinins, Viral, Receptors, Virus, Sialic Acids.
- chemical , pharmacology : Neuraminidase.
- chemical , ultrastructure : Hemagglutinins, Viral.
- metabolism : Orthomyxoviridae.
- Teeft :
- Academic press, Binding affinity, Carbohydrate Sequence, Carbonyl oxygen, Conjugate concentration, Influenza, Influenza viruses, Lvanovsky institute, Minimum energy conformation, Models, Molecular, Molecular modeling, Neu5ac, Paulson, Protein Binding, Reaction mixture, Same time, Seed stocks, Short communications, Sialic acid, Structural model, Structure-Activity Relationship, Substitution, Virology, Virus, alpha-Macroglobulins.
Abstract
Abstract: Equine α2 macroglobulin (EM), known to contain both Neu5Ac and Neu4,5Ac2 sialic acid residues, was treated with Vibrio cholerae sialidase for the selective removal of Neu5Ac and was compared with the untreated EM for its binding by a panel of influenza viruses. Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.
Url:
DOI: 10.1016/0042-6822(92)90541-V
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000194
- to stream Istex, to step Curation: 000194
- to stream Istex, to step Checkpoint: 000C97
- to stream Main, to step Merge: 002042
- to stream PubMed, to step Corpus: 000434
- to stream PubMed, to step Curation: 000434
- to stream PubMed, to step Checkpoint: 000392
- to stream Ncbi, to step Merge: 000081
- to stream Ncbi, to step Curation: 000081
- to stream Ncbi, to step Checkpoint: 000081
- to stream Main, to step Merge: 002020
- to stream Main, to step Curation: 001F46
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant</title><author><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. N. Matrosovich</name></author><author><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name></author><author><name sortKey="Chumakov, M P" sort="Chumakov, M P" uniqKey="Chumakov M" first="M. P." last="Chumakov">M. P. Chumakov</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:FDD06B9D857461945014F05A3F65118AA3EC6964</idno><date when="1992" year="1992">1992</date><idno type="doi">10.1016/0042-6822(92)90541-V</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-FHTL5JF9-7/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000194</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000194</idno><idno type="wicri:Area/Istex/Curation">000194</idno><idno type="wicri:Area/Istex/Checkpoint">000C97</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000C97</idno><idno type="wicri:doubleKey">0042-6822:1992:Matrosovich M:influenza:viruses:differ</idno><idno type="wicri:Area/Main/Merge">002042</idno><idno type="wicri:source">PubMed</idno><idno type="RBID">pubmed:1374985</idno><idno type="wicri:Area/PubMed/Corpus">000434</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000434</idno><idno type="wicri:Area/PubMed/Curation">000434</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000434</idno><idno type="wicri:Area/PubMed/Checkpoint">000392</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000392</idno><idno type="wicri:Area/Ncbi/Merge">000081</idno><idno type="wicri:Area/Ncbi/Curation">000081</idno><idno type="wicri:Area/Ncbi/Checkpoint">000081</idno><idno type="wicri:doubleKey">0042-6822:1992:Matrosovich M:influenza:viruses:differ</idno><idno type="wicri:Area/Main/Merge">002020</idno><idno type="wicri:Area/Main/Curation">001F46</idno><idno type="wicri:Area/Main/Exploration">001F46</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant</title><author><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. N. Matrosovich</name><affiliation wicri:level="1"><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782</wicri:regionArea><wicri:noRegion>Moscow Region 142 782</wicri:noRegion></affiliation></author><author><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name><affiliation wicri:level="1"><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782</wicri:regionArea><wicri:noRegion>Moscow Region 142 782</wicri:noRegion></affiliation></author><author><name sortKey="Chumakov, M P" sort="Chumakov, M P" uniqKey="Chumakov M" first="M. P." last="Chumakov">M. P. Chumakov</name><affiliation wicri:level="1"><country xml:lang="fr">Russie</country><wicri:regionArea>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142 782</wicri:regionArea><wicri:noRegion>Moscow Region 142 782</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="1992">1992</date><biblScope unit="volume">188</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="854">854</biblScope><biblScope unit="page" to="858">858</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>Carbohydrate Sequence</term><term>Hemagglutinins, Viral (metabolism)</term><term>Hemagglutinins, Viral (ultrastructure)</term><term>Models, Molecular</term><term>Neuraminidase (pharmacology)</term><term>Orthomyxoviridae (metabolism)</term><term>Protein Binding</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Sialic Acids (chemistry)</term><term>Sialic Acids (metabolism)</term><term>Structure-Activity Relationship</term><term>alpha-Macroglobulins</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sialiques ()</term><term>Acides sialiques (métabolisme)</term><term>Hémagglutinines virales (métabolisme)</term><term>Hémagglutinines virales (ultrastructure)</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Orthomyxoviridae (métabolisme)</term><term>Relation structure-activité</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Sialidase (pharmacologie)</term><term>Séquence glucidique</term><term>alpha-Macroglobulines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Receptors, Virus</term><term>Sialic Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinins, Viral</term><term>Receptors, Virus</term><term>Sialic Acids</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Hemagglutinins, Viral</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sialiques</term><term>Hémagglutinines virales</term><term>Orthomyxoviridae</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Hémagglutinines virales</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Binding affinity</term><term>Carbohydrate Sequence</term><term>Carbonyl oxygen</term><term>Conjugate concentration</term><term>Influenza</term><term>Influenza viruses</term><term>Lvanovsky institute</term><term>Minimum energy conformation</term><term>Models, Molecular</term><term>Molecular modeling</term><term>Neu5ac</term><term>Paulson</term><term>Protein Binding</term><term>Reaction mixture</term><term>Same time</term><term>Seed stocks</term><term>Short communications</term><term>Sialic acid</term><term>Structural model</term><term>Structure-Activity Relationship</term><term>Substitution</term><term>Virology</term><term>Virus</term><term>alpha-Macroglobulins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acides sialiques</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Relation structure-activité</term><term>Récepteurs viraux</term><term>Séquence glucidique</term><term>alpha-Macroglobulines</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Equine α2 macroglobulin (EM), known to contain both Neu5Ac and Neu4,5Ac2 sialic acid residues, was treated with Vibrio cholerae sialidase for the selective removal of Neu5Ac and was compared with the untreated EM for its binding by a panel of influenza viruses. Type A H3N2 virus strains having Leu in position 226 of their hemagglutinin (HA) changed the affinity for sialidase-treated EM only slightly, if at all, indicative of their ability to bind the 4-0-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1 N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gin studied were unable to recognize Neu4,5Ac2 moieties of EM. Molecular modeling based on the known 3-D structure of H3 HA complexed with sialyllactose (Weis et al. (1988) Nature 333, 426–431) predicts that the 4-0-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</div></front></TEI><affiliations><list><country><li>Russie</li></country></list><tree><country name="Russie"><noRegion><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. N. Matrosovich</name></noRegion><name sortKey="Chumakov, M P" sort="Chumakov, M P" uniqKey="Chumakov M" first="M. P." last="Chumakov">M. P. Chumakov</name><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001F46 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001F46 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:FDD06B9D857461945014F05A3F65118AA3EC6964
|texte= Influenza viruses differ in recognition of 4- O -acetyl substitution of sialic acid receptor determinant
}}
| This area was generated with Dilib version V0.6.33. |  |