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Infect. Immun., 05 1995, 1810-1819, Vol 63, No. 5
T Belay and R Cherniak
The competitive binding specificities of glucuronoxylomannan (GXM) and its
derivatives to factor sera of Cryptococcus neoformans were studied by
enzyme-linked immunosorbent assay. An effort was made to determine the
epitope specificity of each factor serum. Despite the presence of antigenic
factor 1 on all serotypes of C. neoformans, variations in inhibition
ability were observed with different GXMs. The panspecific component of
factor serum 1 (antibody 1) appeared to be due to the presence of more than
one antibody component. The activity was dependent on the 6-O-acetyl
substituent. GXMs of serotypes A and D inhibited factor serum 2 equally
well, indicating a low titer for the antibody 7 component. Serotype B GXM
was a poor inhibitor, and serotype C GXM did not inhibit factor serum 2.
The activity of factor serum 2 was 6-O-acetyl dependent. GXMs from typical
serotype A and serotype D isolates were excellent inhibitors of factor
serum 3. GXMs from serotype B were poorly inhibitory and serotype C did not
inhibit factor serum 3. The activity of factor serum 3 was 6-O-acetyl
dependent. The activity of factor serum 4 was due predominantly to antibody
component 6. The activity of factor 4 was directed mainly against serotype
C, and it was independent of 6-O-acetyl substitution Factor serum 5 was
specific for serotype B GXMs. The inhibitory effect was independent of
6-O-acetyl substitution, but the effect was diminished by reduction of the
glucuronic acid. The GXMs with a typical serotype C structure inhibited
antibody 6. O deacetylation of the GXMs did not affect their inhibitory
activity. However, reduction of glucuronic acid reduced factor serum 6
binding. Factor serum 8 was specific to serotype D; native GXMs of serotype
A were slightly inhibitory. O deacetylation of the serotype D GXMs
abrogated the inhibitory effect. O deacetylation alone abrogates the
activity of antibody components 1, 2, 3, and 8. Reduction of glucuronic
acid reduces the inhibitory activity of the GXM to antibody components 4,
5, and 6. Partial GXM structures and methyl glycosides did not effectively
inhibit the activity of any of the factor sera.
Copyright © 1995, American Society for Microbiology
Determination of antigen binding specificities of Cryptococcus neoformans factor sera by enzyme-linked immunosorbent assay
Department of Chemistry, Georgia State University, Atlanta 30303, USA.
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