Effects of altered N-glycan structures of Cryptococcus neoformans mannoproteins, MP98 (Cda2) and MP84 (Cda3), on interaction with host cellsopen access
- Authors
- Lee, Su-Bin; Mota, Catia; Thak, Eun Jung; Kim, Jungho; Son, Ye Ji; Oh, Doo-Byoung; Kang, Hyun Ah
- Issue Date
- Jan-2023
- Publisher
- Nature Research
- Citation
- Scientific Reports, v.13, no.1
- Journal Title
- Scientific Reports
- Volume
- 13
- Number
- 1
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66278
- DOI
- 10.1038/s41598-023-27422-9
- ISSN
- 2045-2322
- Abstract
- Cryptococcus neoformans is an opportunistic human fungal pathogen causing lethal meningoencephalitis. It has several cell wall mannoproteins (MPs) identified as immunoreactive antigens. To investigate the structure and function of N-glycans assembled on cryptococcal cell wall MPs in host cell interactions, we purified MP98 (Cda2) and MP84 (Cda3) expressed in wild-type (WT) and N-glycosylation-defective alg3 mutant (alg3Δ) strains. HPLC and MALDI-TOF analysis of the MP proteins from the WT revealed protein-specific glycan structures with different extents of hypermannosylation and xylose/xylose phosphate addition. In alg3Δ, MP98 and MP84 had truncated core N-glycans, containing mostly five and seven mannoses (M5 and M7 forms), respectively. In vitro adhesion and uptake assays indicated that the altered core N-glycans did not affect adhesion affinities to host cells although the capacity to induce the immune response of bone-marrow derived dendritic cells (BMDCs) decreased. Intriguingly, the removal of all N-glycosylation sites on MP84 increased adhesion to host cells and enhanced the induction of cytokine secretion from BMDCs compared with that on MP84 carrying WT N-glycans. Therefore, the structure-dependent effects of N-glycans suggested their complex roles in modulating the interaction of MPs with host cells to avoid nonspecific adherence to host cells and host immune response hyperactivation. © 2023, The Author(s).
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