Interactions of Surfactant Protein a with Influenza A Viruses: Binding and Neutralization
| Autor: | L.M.G. Van Golde, Martin C. Harmsen, Jan Verhoef, E. Brouwer, C. A. Benne, J. A. G. Van Strijp, J. F. Van Iwaarden, C. A. Kraaijeveld |
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| Rok vydání: | 1995 |
| Předmět: |
Pulmonary Surfactant-Associated Proteins
Proteolipids viruses Orthomyxoviridae Oligosaccharides Antibodies Viral Virus Replication medicine.disease_cause Immunoenzyme Techniques chemistry.chemical_compound C-type lectin Influenza A virus medicine Animals Humans Immunology and Allergy Fluorometry Fluorescein isothiocyanate Cells Cultured Pulmonary Surfactant-Associated Protein A Dose-Response Relationship Drug biology Antibodies Monoclonal virus diseases Pulmonary Surfactants biology.organism_classification respiratory tract diseases Sialic acid Infectious Diseases chemistry Biochemistry biology.protein Neuraminidase N-Acetylneuraminic acid Fluorescein-5-isothiocyanate Protein Binding |
| Zdroj: | Journal of Infectious Diseases. 171:335-341 |
| ISSN: | 1537-6613 0022-1899 |
| DOI: | 10.1093/infdis/171.2.335 |
| Popis: | The interaction of pulmonary surfactant protein A (SP-A) with influenza A H1N1 and H3N2 viruses was investigated. SP-A is a sialated C type lectin with affinity for mannose residues. Flow cytometry showed that binding of fluorescein isothiocyanate (FITC)-labeled SP-A to H3N2 virus-infected cells was specific and time- and concentration-dependent. Oligosaccharides did not affect the binding of FITC-SP-A to the infected cells. Preincubation of H1N1 and H3N2 with SP-A resulted in a dose-dependent reduction of the infectivity of the viruses to cells. Removal of the carbohydrate moiety of SP-A by N-glycosidase F or cleavage of its sialic acid residues by neuraminidase prevented the interactions of SP-A with the viruses. It is concluded that SP-A binds to influenza A viruses via its sialic acid residues and, thereby, neutralizes the virus. |
| Databáze: | OpenAIRE |
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