Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant.
Identifieur interne : 000081 ( Ncbi/Merge ); précédent : 000080; suivant : 000082Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant.
Auteurs : M N Matrosovich ; A S Gambaryan ; M P ChumakovSource :
- 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.
- Carbohydrate Sequence, Models, Molecular, Protein Binding, Structure-Activity Relationship, alpha-Macroglobulins.
Abstract
Equine alpha 2-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-O-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gln 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-O-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.
DOI: 10.1016/0042-6822(92)90541-v
PubMed: 1374985
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Sciences, Moscow Region.</nlm:affiliation><wicri:noCountry code="subField">Moscow Region</wicri:noCountry></affiliation></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></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></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="MESH" xml:lang="en"><term>Carbohydrate Sequence</term><term>Models, Molecular</term><term>Protein Binding</term><term>Structure-Activity Relationship</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></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Equine alpha 2-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-O-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gln 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-O-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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1374985</PMID><DateCompleted><Year>1992</Year><Month>06</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>188</Volume><Issue>2</Issue><PubDate><Year>1992</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant.</ArticleTitle><Pagination><MedlinePgn>854-8</MedlinePgn></Pagination><Abstract><AbstractText>Equine alpha 2-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-O-Ac-substituted Neu5Ac receptor determinant. At the same time, all B and H1N1 viruses, some H2N2 variants, as well as H3N2 strains with 226 Gln 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-O-Ac substituent of sialic acid would protrude with its carbonyl oxygen inside the receptor-binding site of HA, thus possibly interfering with binding.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Matrosovich</LastName><ForeName>M N</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gambaryan</LastName><ForeName>A S</ForeName><Initials>AS</Initials></Author><Author ValidYN="Y"><LastName>Chumakov</LastName><ForeName>M P</ForeName><Initials>MP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006389">Hemagglutinins, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012794">Sialic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000511">alpha-Macroglobulins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002240" MajorTopicYN="N">Carbohydrate Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006389" MajorTopicYN="N">Hemagglutinins, Viral</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009975" MajorTopicYN="N">Orthomyxoviridae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012794" MajorTopicYN="N">Sialic Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000511" MajorTopicYN="N">alpha-Macroglobulins</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>6</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>6</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>6</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1374985</ArticleId><ArticleId IdType="pii">0042-6822(92)90541-V</ArticleId><ArticleId IdType="doi">10.1016/0042-6822(92)90541-v</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><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><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M N" last="Matrosovich">M N Matrosovich</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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