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영어
Cryptococcus neoformans is the opportunistic human-pathogenic fungus causing life-threatening meningoencephalitis in immunocompromised patients, especially patients with AIDS. Several C. neoformans mannoproteins, such as chitin deacetylase 2 (MP98), are reported as key antigens stimulating host T-cell response. Here, we analyzed the glycosylation pattern of protein , MP98(H), in the wild-type and various glycosylation mutant strains of C. neoformans. The apparent molecular weight (MW) of MP98(H)wassignificantly decreasedin the alg3Δ strain, which has defects in biosynthesis of N-glycans, but not in the O-glycosylation mutants. The MW of MP98(H) secreted from wild type and glycosylation mutant strains was converted to its predicted size after N-glycosidase treatment, supporting that MP98(H) is highly modified by N-glycosylation. We further investigated the function of in vitro adhesion assayMP98(H) proteins from the wild type and alg3Δ strains. Unexpectedly, the alg3Δ/MP98(H) protein, bearing short N glycans, adhered more intensely to the lung cells than the WT/MP98(H) protein, bearing high-mannose type N-glycans, indicating that truncated N-glycans rather enhanced adhesion of MP98(H) to epithelial lung cells. These results strongly indicate that N-glycan structure of MP98 affects the adhesion efficiency of C. neoformans to host cells.