Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro.
Identifieur interne : 000389 ( PubMed/Corpus ); précédent : 000388; suivant : 000390Serum amyloid P component binds to influenza A virus haemagglutinin and inhibits the virus infection in vitro.
Auteurs : O. Andersen ; K. Vilsgaard Ravn ; I. Juul S Rensen ; G. Jonson ; E. Holm Nielsen ; S E SvehagSource :
- Scandinavian journal of immunology [ 0300-9475 ] ; 1997.
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
Links to Exploration step
pubmed:9350282Le document en format XML
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<author><name sortKey="Andersen, O" sort="Andersen, O" uniqKey="Andersen O" first="O" last="Andersen">O. Andersen</name>
<affiliation><nlm:affiliation>Department of Infectious Diseases, Odense University, Denmark.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Vilsgaard Ravn, K" sort="Vilsgaard Ravn, K" uniqKey="Vilsgaard Ravn K" first="K" last="Vilsgaard Ravn">K. Vilsgaard Ravn</name>
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<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>
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<author><name sortKey="Jonson, G" sort="Jonson, G" uniqKey="Jonson G" first="G" last="Jonson">G. Jonson</name>
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<author><name sortKey="Holm Nielsen, E" sort="Holm Nielsen, E" uniqKey="Holm Nielsen E" first="E" last="Holm Nielsen">E. Holm Nielsen</name>
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<author><name sortKey="Svehag, S E" sort="Svehag, S E" uniqKey="Svehag S" first="S E" last="Svehag">S E Svehag</name>
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<term>Antiviral Agents (metabolism)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Blotting, Western</term>
<term>Cell Line</term>
<term>Cell Membrane (metabolism)</term>
<term>Cell Membrane (ultrastructure)</term>
<term>Dogs</term>
<term>Glycosaminoglycans (pharmacology)</term>
<term>Hemagglutination Inhibition Tests</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term>
<term>Hemagglutinins, Viral (drug effects)</term>
<term>Hemagglutinins, Viral (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>
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<term>Hemagglutinin Glycoproteins, Influenza Virus</term>
<term>Hemagglutinins, Viral</term>
<term>Serum Amyloid P-Component</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Influenza A virus</term>
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<term>Influenza A virus</term>
<term>Serum Amyloid P-Component</term>
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<term>Blotting, Western</term>
<term>Cell Line</term>
<term>Dogs</term>
<term>Hemagglutination Inhibition Tests</term>
<term>Humans</term>
<term>Kidney</term>
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<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>
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<Title>Scandinavian journal of immunology</Title>
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<Abstract><AbstractText>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.</AbstractText>
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