Mannan is one of the major cell wall components in Candida albicans . Previously, we generated a human recombinant IgG1 antimannan antibody known as M1g1 and showed a protective role in host resistance to systemic candidiasis in mice. The purpose of this study was to characterize the epitope of M1g1. Oligomannosides were isolated by thin layer chromatography, and identity was determined by 1H-NMR. Purified oligomannosides were used either as inhibitors of M1g1 binding to mannan in a competition ELISA or as neoglycolipid-conjugates in ELISA for direct binding by M1g1. Furthermore, molecular recognition of oligomannosides by M1g1 was analyzed by 3D modeling and by modification of interacting amino acids with site-directed mutagenesis. Reactivity of serum natural antimannan antibody from normal adults for neoglycolipid-conjugated oligomannosides was determined by ELISA. β-1,2-linked mannotriose is the specific epitope for the protective human recombinant antimannan antibody M1g1 and is reactive with natural antimannan antibody found in normal individuals, suggesting the presence of naturally occurring protective antimannan antibody.
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 49/04M, Masters Abstracts International|
|Subjects:||Molecular biology, Microbiology, Biochemistry|
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