Purification and characterization of the extracellular C3d-binding protein of Candida albicans.

摘要: Abstract A C3d-binding glycoprotein was purified from the culture filtrate of Candida albicans by preparative isoelectric focusing. The protein possessed a pI 3.9 to 4.1 and could inhibit rosetting EAC3d (sheep erythrocytes conjugated C3d) pseudohyphae C. albicans. When analyzed polyacrylamide gel electrophoresis in presence sodium dodecyl sulfate mercaptoethanol, migrated as doublet with apparent molecular masses 55 60 kilodaltons (kDa) 50-kDa band nonreducing gels. These results were observed Aurodye stain for proteins. Western immunoblot, concanavalin A stain, which indicates that both bands contain carbohydrate well antigenic determinants. treatment endoglycosidase F but not endoglycosidases H, N, O resulted complete conversion into faster-migrating broad an mass 45 kDa. amino acid analysis compared CR2 B lymphocytes, significant differences observed. data indicate secretes during growth vitro appears be different mammalian C3d receptor.