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10.1002/eji.1830270413

http://scihub22266oqcxt.onion/10.1002/eji.1830270413
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9130640!ä!9130640

suck abstract from ncbi


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pmid9130640      Eur+J+Immunol 1997 ; 27 (4): 886-90
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  • Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages #MMPMID9130640
  • Benne CA; Benaissa-Trouw B; van Strijp JA; Kraaijeveld CA; van Iwaarden JF
  • Eur J Immunol 1997[Apr]; 27 (4): 886-90 PMID9130640show ga
  • Surfactant protein A (SP-A) and surfactant protein D (SP-D) are collectins, and both proteins were shown to interact with influenza A virus and alveolar macrophages. However, it is not known whether SP-A and SP-D can serve as opsonins for the phagocytosis of influenza A virus by alveolar macrophages. In the present study, we investigated the opsonic activities of SP-A and SP-D for phagocytosis of fluorescein isothiocyanate (FITC)-labeled influenza A (H3N2) virus by rat alveolar macrophages using flow cytometry. SP-A enhanced the association of the virus with macrophages in a dose-dependent manner, reaching a maximum at an SP-A concentration of 60 microg/ml. An approximate threefold increase in association of influenza A virus with alveolar macrophages in the presence of SP-A over control incubations which contained no SP-A was observed. Half of the total cell-associated fluorescence could be quenched as demonstrated using the extracellular quenching dye trypan blue. These results indicate that SP-A mediates internalization of FITC-labeled influenza A (H3N2) virus by alveolar macrophages. Removal of the carbohydrate moiety of SP-A by N-glycosidase F treatment or cleavage of its sialic acid residues by neuraminidase abolished the enhancement of the phagocytosis of FITC-labeled influenza A virus by alveolar macrophages. Mannan, a mannose homopolysaccharide known to bind to the carbohydrate-binding domain of SP-A, did not affect the SP-A-mediated phagocytosis of FITC-labeled influenza by alveolar macrophages. In contrast, SP-D neither enhanced the association of FITC-labeled influenza A virus with alveolar macrophages nor affected the opsonic activity of SP-A for FITC-labeled influenza A (H3N2) virus at the SP-D concentrations tested. It is concluded that SP-A acts via its sialic acid residues as an opsonin in the phagocytosis of influenza A virus by alveolar macrophages.
  • |Animals[MESH]
  • |Carrier Proteins/*immunology/physiology[MESH]
  • |Fluorescein-5-isothiocyanate[MESH]
  • |Glycoproteins/*immunology/physiology[MESH]
  • |Humans[MESH]
  • |Influenza A virus/*immunology[MESH]
  • |Macrophages, Alveolar/*immunology[MESH]
  • |Male[MESH]
  • |Oligosaccharides/pharmacology[MESH]
  • |Opsonin Proteins/*physiology[MESH]
  • |Phagocytosis/*drug effects[MESH]
  • |Proteolipids/*immunology/physiology[MESH]
  • |Pulmonary Surfactant-Associated Protein A[MESH]
  • |Pulmonary Surfactant-Associated Protein D[MESH]
  • |Pulmonary Surfactant-Associated Proteins[MESH]
  • |Pulmonary Surfactants/*immunology/physiology[MESH]
  • |Rats[MESH]


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