Linked Life Data

9130640

Source:http://linkedlifedata.com/resource/pubmed/id/9130640

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-5-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
886-90
pubmed:dateRevised
2005-11-22
pubmed:meshHeading
pubmed-meshheading:9130640-Animals, pubmed-meshheading:9130640-Carrier Proteins, pubmed-meshheading:9130640-Fluorescein-5-isothiocyanate, pubmed-meshheading:9130640-Glycoproteins, pubmed-meshheading:9130640-Humans, pubmed-meshheading:9130640-Influenza A virus, pubmed-meshheading:9130640-Macrophages, Alveolar, pubmed-meshheading:9130640-Male, pubmed-meshheading:9130640-Oligosaccharides, pubmed-meshheading:9130640-Opsonin Proteins, pubmed-meshheading:9130640-Phagocytosis, pubmed-meshheading:9130640-Proteolipids, pubmed-meshheading:9130640-Pulmonary Surfactant-Associated Protein A, pubmed-meshheading:9130640-Pulmonary Surfactant-Associated Protein D, pubmed-meshheading:9130640-Pulmonary Surfactant-Associated Proteins, pubmed-meshheading:9130640-Pulmonary Surfactants, pubmed-meshheading:9130640-Rats, pubmed-meshheading:9130640-Rats, Wistar
pubmed:year
1997
pubmed:articleTitle
Surfactant protein A, but not surfactant protein D, is an opsonin for influenza A virus phagocytosis by rat alveolar macrophages.
pubmed:affiliation
Regional Public Health Laboratory Groningen, The Netherlands.
pubmed:publicationType
Journal Article