Serum Amyloid P Component Binds to Influenza A Virus Haemagglutinin and Inhibits the Virus Infection In Vitro
| Autor: | I. Juul SØRensen, Ove Andersen, S.-E. Svehag, K Vilsgaard Ravn, E. Holm Nielsen, G Jonson |
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| Rok vydání: | 1997 |
| Předmět: |
Protein Denaturation
Acetylgalactosamine genetic structures viruses Blotting Western Immunology Hemagglutinins Viral Mannose Hemagglutinin Glycoproteins Influenza Virus Plasma protein binding Biology Kidney medicine.disease_cause Antiviral Agents Virus Cell Line chemistry.chemical_compound Dogs Orthomyxoviridae Infections Viral envelope Influenza A virus medicine Animals Humans Serum amyloid P component Glycosaminoglycans Pentraxins Cell Membrane Monosaccharides General Medicine Heparan sulfate Hemagglutination Inhibition Tests eye diseases Serum Amyloid P-Component Biochemistry chemistry biology.protein Protein Binding |
| Zdroj: | Scandinavian Journal of Immunology. 46:331-337 |
| ISSN: | 1365-3083 0300-9475 |
| DOI: | 10.1046/j.1365-3083.1997.d01-147.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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