Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro.
Identifieur interne : 001B24 ( Main/Exploration ); précédent : 001B23; suivant : 001B25Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro.
Auteurs : O. Andersen [Danemark] ; K. Vilsgaard Ravn ; I. Juul S Rensen ; G. Jonson ; E. Holm Nielsen ; S E SvehagSource :
- Scandinavian journal of immunology [ 0300-9475 ] ; 1997.
Descripteurs français
- KwdFr :
- Acétyl-galactosamine (pharmacologie), Animaux, Antiviraux (métabolisme), Antiviraux (pharmacologie), Chiens, Composant sérique amyloïde P (métabolisme), Composant sérique amyloïde P (physiologie), Composant sérique amyloïde P (ultrastructure), Dénaturation des protéines, Glycoprotéine hémagglutinine du virus influenza (métabolisme), Glycosaminoglycanes (pharmacologie), Humains, Hémagglutinines virales (), Hémagglutinines virales (métabolisme), Infections à Orthomyxoviridae (), Infections à Orthomyxoviridae (immunologie), Infections à Orthomyxoviridae (virologie), Liaison aux protéines, Lignée cellulaire, Membrane cellulaire (métabolisme), Membrane cellulaire (ultrastructure), Oses (pharmacologie), Rein, Technique de Western, Tests d'inhibition de l'hémagglutination, Virus de la grippe A (), Virus de la grippe A (métabolisme), Virus de la grippe A (ultrastructure).
- MESH :
- immunologie : Infections à Orthomyxoviridae.
- métabolisme : Antiviraux, Composant sérique amyloïde P, Glycoprotéine hémagglutinine du virus influenza, Hémagglutinines virales, Membrane cellulaire, Virus de la grippe A.
- pharmacologie : Acétyl-galactosamine, Antiviraux, Glycosaminoglycanes, Oses.
- physiologie : Composant sérique amyloïde P.
- virologie : Infections à Orthomyxoviridae.
- Animaux, Chiens, Composant sérique amyloïde P, Dénaturation des protéines, Humains, Hémagglutinines virales, Infections à Orthomyxoviridae, Liaison aux protéines, Lignée cellulaire, Membrane cellulaire, Rein, Technique de Western, Tests d'inhibition de l'hémagglutination, Virus de la grippe A.
English descriptors
- KwdEn :
- Acetylgalactosamine (pharmacology), Animals, Antiviral Agents (metabolism), Antiviral Agents (pharmacology), Blotting, Western, Cell Line, Cell Membrane (metabolism), Cell Membrane (ultrastructure), Dogs, Glycosaminoglycans (pharmacology), Hemagglutination Inhibition Tests, Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Hemagglutinins, Viral (drug effects), Hemagglutinins, Viral (metabolism), Humans, Influenza A virus (drug effects), Influenza A virus (metabolism), Influenza A virus (ultrastructure), Kidney, Monosaccharides (pharmacology), Orthomyxoviridae Infections (immunology), Orthomyxoviridae Infections (prevention & control), Orthomyxoviridae Infections (virology), Protein Binding, Protein Denaturation, Serum Amyloid P-Component (metabolism), Serum Amyloid P-Component (physiology), Serum Amyloid P-Component (ultrastructure).
- MESH :
- chemical , drug effects : Hemagglutinins, Viral.
- chemical , metabolism : Antiviral Agents, Hemagglutinin Glycoproteins, Influenza Virus, Hemagglutinins, Viral, Serum Amyloid P-Component.
- chemical , pharmacology : Acetylgalactosamine, Antiviral Agents, Glycosaminoglycans, Monosaccharides.
- drug effects : Influenza A virus.
- immunology : Orthomyxoviridae Infections.
- metabolism : Cell Membrane, Influenza A virus.
- chemical , physiology : Serum Amyloid P-Component.
- prevention & control : Orthomyxoviridae Infections.
- ultrastructure : Cell Membrane, Influenza A virus, Serum Amyloid P-Component.
- virology : Orthomyxoviridae Infections.
- Animals, Blotting, Western, Cell Line, Dogs, Hemagglutination Inhibition Tests, Humans, Kidney, Protein Binding, Protein Denaturation.
Abstract
Serum amyloid P component (SAP) is a member of the phylogenetically conserved and structurally related group of proteins called pentraxins. SAP exhibits multispecific calcium-dependent binding to oligosaccharides with terminal N-acetyl-galactosamine, mannose and glucuronic acid. The authors report that SAP can bind to influenza A virus and inhibit agglutination of erythrocytes mediated by the virus subtypes H1N1, H2N2 and H3N2. SAP also inhibits the production of haemagglutinin (HA) an the cytopathogenic effect of influenza A virus in MDCK cells. The binding of SAP to the virus requires physiological calcium concentrations and is blocked by specific SAP antibodies. Denaturated and renaturated SAP retained inhibition of HA. Electron microscopy shows Ca(2+)-dependent binding of SAP to spikes on the viral envelope and immunoblotting indicates that SAP binds to a 50-55 kDa peptide corresponding to the mass of the HA1 peptide. Of several monosaccharides tested only D-mannose interfered with SAP's inhibition of both HA and infectivity. The glycosaminoglycans heparan sulfate and heparin, which bind SAP, reduced SAPs binding to the virus. The results indicate that the inhibition by SAP is due to steric effects when SAP binds to terminal mannose on oligosaccharides localized close to the sialic acid-binding site of the HA trimer.
DOI: 10.1046/j.1365-3083.1997.d01-147.x
PubMed: 9350282
Affiliations:
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Le document en format XML
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Juul S Rensen</name></author><author><name sortKey="Jonson, G" sort="Jonson, G" uniqKey="Jonson G" first="G" last="Jonson">G. Jonson</name></author><author><name sortKey="Holm Nielsen, E" sort="Holm Nielsen, E" uniqKey="Holm Nielsen E" first="E" last="Holm Nielsen">E. Holm Nielsen</name></author><author><name sortKey="Svehag, S E" sort="Svehag, S E" uniqKey="Svehag S" first="S E" last="Svehag">S E Svehag</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9350282</idno><idno type="pmid">9350282</idno><idno type="doi">10.1046/j.1365-3083.1997.d01-147.x</idno><idno type="wicri:Area/PubMed/Corpus">000389</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000389</idno><idno type="wicri:Area/PubMed/Curation">000389</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000389</idno><idno type="wicri:Area/PubMed/Checkpoint">000354</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000354</idno><idno type="wicri:Area/Ncbi/Merge">001351</idno><idno type="wicri:Area/Ncbi/Curation">001351</idno><idno type="wicri:Area/Ncbi/Checkpoint">001351</idno><idno type="wicri:doubleKey">0300-9475:1997:Andersen O:serum:amyloid:p</idno><idno type="wicri:Area/Main/Merge">001B84</idno><idno type="wicri:Area/Main/Curation">001B24</idno><idno type="wicri:Area/Main/Exploration">001B24</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro.</title><author><name sortKey="Andersen, O" sort="Andersen, O" uniqKey="Andersen O" first="O" last="Andersen">O. Andersen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Infectious Diseases, Odense University, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Department of Infectious Diseases, Odense University</wicri:regionArea><wicri:noRegion>Odense University</wicri:noRegion></affiliation></author><author><name sortKey="Vilsgaard Ravn, K" sort="Vilsgaard Ravn, K" uniqKey="Vilsgaard Ravn K" first="K" last="Vilsgaard Ravn">K. Vilsgaard Ravn</name></author><author><name sortKey="Juul S Rensen, I" sort="Juul S Rensen, I" uniqKey="Juul S Rensen I" first="I" last="Juul S Rensen">I. Juul S Rensen</name></author><author><name sortKey="Jonson, G" sort="Jonson, G" uniqKey="Jonson G" first="G" last="Jonson">G. Jonson</name></author><author><name sortKey="Holm Nielsen, E" sort="Holm Nielsen, E" uniqKey="Holm Nielsen E" first="E" last="Holm Nielsen">E. 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(metabolism)</term><term>Humans</term><term>Influenza A virus (drug effects)</term><term>Influenza A virus (metabolism)</term><term>Influenza A virus (ultrastructure)</term><term>Kidney</term><term>Monosaccharides (pharmacology)</term><term>Orthomyxoviridae Infections (immunology)</term><term>Orthomyxoviridae Infections (prevention & control)</term><term>Orthomyxoviridae Infections (virology)</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Serum Amyloid P-Component (metabolism)</term><term>Serum Amyloid P-Component (physiology)</term><term>Serum Amyloid P-Component (ultrastructure)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acétyl-galactosamine (pharmacologie)</term><term>Animaux</term><term>Antiviraux (métabolisme)</term><term>Antiviraux (pharmacologie)</term><term>Chiens</term><term>Composant sérique amyloïde P (métabolisme)</term><term>Composant sérique amyloïde P (physiologie)</term><term>Composant sérique amyloïde P (ultrastructure)</term><term>Dénaturation des protéines</term><term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term><term>Glycosaminoglycanes (pharmacologie)</term><term>Humains</term><term>Hémagglutinines virales ()</term><term>Hémagglutinines virales (métabolisme)</term><term>Infections à Orthomyxoviridae ()</term><term>Infections à Orthomyxoviridae (immunologie)</term><term>Infections à Orthomyxoviridae (virologie)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Membrane cellulaire (métabolisme)</term><term>Membrane cellulaire (ultrastructure)</term><term>Oses (pharmacologie)</term><term>Rein</term><term>Technique de Western</term><term>Tests d'inhibition de l'hémagglutination</term><term>Virus de la grippe A ()</term><term>Virus de la grippe A (métabolisme)</term><term>Virus de la grippe A (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Hemagglutinins, 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qualifier="virologie" xml:lang="fr"><term>Infections à Orthomyxoviridae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Cell Line</term><term>Dogs</term><term>Hemagglutination Inhibition Tests</term><term>Humans</term><term>Kidney</term><term>Protein Binding</term><term>Protein Denaturation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chiens</term><term>Composant sérique amyloïde P</term><term>Dénaturation des protéines</term><term>Humains</term><term>Hémagglutinines virales</term><term>Infections à Orthomyxoviridae</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Membrane cellulaire</term><term>Rein</term><term>Technique de Western</term><term>Tests d'inhibition de l'hémagglutination</term><term>Virus de la grippe A</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Serum amyloid P component (SAP) is a member of the phylogenetically conserved and structurally related group of proteins called pentraxins. SAP exhibits multispecific calcium-dependent binding to oligosaccharides with terminal N-acetyl-galactosamine, mannose and glucuronic acid. The authors report that SAP can bind to influenza A virus and inhibit agglutination of erythrocytes mediated by the virus subtypes H1N1, H2N2 and H3N2. SAP also inhibits the production of haemagglutinin (HA) an the cytopathogenic effect of influenza A virus in MDCK cells. The binding of SAP to the virus requires physiological calcium concentrations and is blocked by specific SAP antibodies. Denaturated and renaturated SAP retained inhibition of HA. Electron microscopy shows Ca(2+)-dependent binding of SAP to spikes on the viral envelope and immunoblotting indicates that SAP binds to a 50-55 kDa peptide corresponding to the mass of the HA1 peptide. Of several monosaccharides tested only D-mannose interfered with SAP's inhibition of both HA and infectivity. The glycosaminoglycans heparan sulfate and heparin, which bind SAP, reduced SAPs binding to the virus. The results indicate that the inhibition by SAP is due to steric effects when SAP binds to terminal mannose on oligosaccharides localized close to the sialic acid-binding site of the HA trimer.</div></front></TEI><affiliations><list><country><li>Danemark</li></country></list><tree><noCountry><name sortKey="Holm Nielsen, E" sort="Holm Nielsen, E" uniqKey="Holm Nielsen E" first="E" last="Holm Nielsen">E. Holm Nielsen</name><name sortKey="Jonson, G" sort="Jonson, G" uniqKey="Jonson G" first="G" last="Jonson">G. Jonson</name><name sortKey="Juul S Rensen, I" sort="Juul S Rensen, I" uniqKey="Juul S Rensen I" first="I" last="Juul S Rensen">I. Juul S Rensen</name><name sortKey="Svehag, S E" sort="Svehag, S E" uniqKey="Svehag S" first="S E" last="Svehag">S E Svehag</name><name sortKey="Vilsgaard Ravn, K" sort="Vilsgaard Ravn, K" uniqKey="Vilsgaard Ravn K" first="K" last="Vilsgaard Ravn">K. Vilsgaard Ravn</name></noCountry><country name="Danemark"><noRegion><name sortKey="Andersen, O" sort="Andersen, O" uniqKey="Andersen O" first="O" last="Andersen">O. Andersen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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