beta-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3.
Infect Immun
; 68(8): 4391-8, 2000 Aug.
Article
en En
| MEDLINE
| ID: mdl-10899835
ABSTRACT
beta-1,2-linked oligomannoside residues are present, associated with mannan and a glycolipid, the phospholipomannan, at the Candida albicans cell wall surface. beta-1,2-linked oligomannoside residues act as adhesins for macrophages and stimulate these cells to undergo cytokine production. To characterize the macrophage receptor involved in the recognition of C. albicans beta-1,2-oligomannoside we used the J774 mouse cell line, which is devoid of the receptor specific for alpha-linked mannose residues. A series of experiments based on affinity binding on either C. albicans yeast cells or beta-1,2-oligomannoside-conjugated bovine serum albumin (BSA) and subsequent disclosure with biotinylated conjugated BSA repeatedly led to the detection of a 32-kDa macrophage protein. An antiserum specific for this 32-kDa protein inhibited C. albicans binding to macrophages and was used to immunoprecipitate the molecule. Two high-pressure liquid chromatography-purified peptides from the 32-kDa tryptic digest showed complete homology to galectin-3 (previously designated Mac-2 antigen), an endogenous lectin with pleiotropic functions which is expressed in a wide variety of cell types with which C. albicans interacts as a saprophyte or a parasite.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Oligosacáridos
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Candida albicans
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Antígenos de Diferenciación
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Macrófagos Peritoneales
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Manósidos
Límite:
Animals
Idioma:
En
Revista:
Infect Immun
Año:
2000
Tipo del documento:
Article
País de afiliación:
Francia