Infection and Immunity, August 2000, p. 4391-4398, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
-1,2-Linked Oligomannosides from Candida
albicans Bind to a 32-Kilodalton Macrophage Membrane Protein
Homologous to the Mammalian Lectin Galectin-3
Laboratoire de Mycologie Fondamentale et Appliquée, INSERM E9915, Faculté de Médecine, Pôle Recherche, 59037 Lille Cedex, France
Received 31 January 2000/Returned for modification 10 March 2000/Accepted 26 April 2000
-1,2-linked oligomannoside residues are present, associated with
mannan and a glycolipid, the phospholipomannan, at the Candida albicans cell wall surface.
-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
-1,2-oligomannoside we used the J774 mouse cell line, which is
devoid of the receptor specific for
-linked mannose residues. A
series of experiments based on affinity binding on either C. albicans yeast cells or
-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.
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