PURIFICATION AND CHARACTERIZATION OF THE SEROTYPE-SPECIFIC POLYSACCHARIDE ANTIGEN OF TRICHOSPORON-CUTANEUM SEROTYPE-II - A DISEASE-RELATED ANTIGEN OF JAPANESE SUMMER-TYPE HYPERSENSITIVITY PNEUMONITIS
T. Mizobe et al., PURIFICATION AND CHARACTERIZATION OF THE SEROTYPE-SPECIFIC POLYSACCHARIDE ANTIGEN OF TRICHOSPORON-CUTANEUM SEROTYPE-II - A DISEASE-RELATED ANTIGEN OF JAPANESE SUMMER-TYPE HYPERSENSITIVITY PNEUMONITIS, Clinical and experimental allergy, 25(3), 1995, pp. 265-272
Summer-type hypersensitivity pneumonitis (SHP) is a unique type of hyp
ersensitivity pneumonitis and the most prevalent in Japan. Our previou
s study clarified that the causative agent of the disease is Trichospo
ron cutaneum, and that the patients with SHP have high titres of antib
odies against the serotype-specific antigen of polysaccharide nature w
hich exist in the high molecular weight fraction of the culture supern
atant of the yeast. In this study, we purified the serotype-specific a
ntigen of serotype II T. cutaneum by gel filtration and affinity chrom
atography using a monoclonal antibody, D-8, specific for a high molecu
lar weight antigen of serotype II T. cutaneum, and elucidated the stru
cture of the antigen. This affinity-purified antigen was shown to be a
n essentially acidic polysaccharide comprising mannose, xylose, and gl
ucuronic acid (6:44:4.7). Chemical analysis showed that this polysacch
aride antigen contains a (1-3)linked mannan backbone attached with sho
rt side chains of(1-4)-linked mannose and a small proportion of(1-2)-l
inked xylose residues by substituting the 2- or dr-positions of the (1
-3)-linked mannose residues of the main chain. Approximately one-fifth
of the side chains were terminated with glucuronic acid residues. The
antigenic epitope of the serotype-specific antigen was shown to invol
ve the terminal glucoronic acid residues as revealed by immunodiffusio
n test and sandwich enzyme-linked immunosorbent assay using monoclonal
antibody D-8.