Properties of the major antigens of rat and human Pneumocystis carinii.

摘要: The major rat and human Pneumocystis carinii antigens were analyzed for their susceptibility to treatment with enzymes other procedures by immunoblotting, immunofluorescence, light microscopy. Carbohydrate residues further lectin-binding experiments. 116-kilodalton (kDa) band of P. was susceptible proteolytic (e.g., trypsin) glycolytic Zymolyase) treatments but not a variety lipase). This moiety reacted strongly concanavalin A wheat germ agglutinin, indicating the presence mannosyl or glucosyl N-acetylglucosamine residues. Immunofluorescence staining surface labeling suggested that 116-kDa antigen located on cell wall. 45- 50-kDa bands as sensitive degradative when studied after immobilization onto nitrocellulose more resistant in situ whole organisms. These moieties exhibited poor binding lectins reactivity surface-labeling procedures. appeared be glycoprotein characteristics similar those its counterpart rats, whereas 40-kDa protein carbohydrate properties closely related rat-derived antigens. We conclude are complex glycoproteins this information will helpful developing strategies isolation purification study function.