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Taxonomic group: fungi / Basidiomycota (Phylum: Basidiomycota)
Associated disease: infection due to Cryptococcus neoformans [ICD11: XN3EH

]

The structure was elucidated in this paper
NCBI PubMed ID: 36670130
Publication DOI: 10.1038/s41598-023-27422-9
Journal NLM ID: 101563288
Publisher: London: Nature Publishing Group
Correspondence: H.A. Kang <hyunkang

cau.ac.kr>
Institutions: Department of Life Science, College of Natural Science, Chung-Ang University, Seoul, 156-756, South Korea, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, South Korea, Department of Biosystems and Bioengineering, KRIBB School, University of Science and Technology (UST), Daejeon, 34113, South Korea

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.

structure, N-glycans, Cryptococcus neoformans, cell wall mannoproteins

Structure type: oligomer
Location inside paper: Fig. 2B, Fig. 2D, alg3ΔMP84, Xyl1Man6GlcNAc2
Aglycon: alg3ΔMP84 (Cda3) protein
Trivial name: cell wall mannoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_141793,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_241100,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_55,SB_67,SB_72,SB_73,SB_74,SB_85

Methods: SDS-PAGE, DNA techniques, Western blotting, MALDI-TOF MS, HPLC, protein detection, cytokine production
Comments, role: the minor glycan expressed in recombinant alg3ΔMP84 strain
3D data: 3D data

Related record ID(s): 41053, 41425, 41426
NCBI Taxonomy refs (TaxIDs): 5207
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There are 96 chemically distinct structures. Please, select:

CC(=O)N[C@H]1[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O[C@H]3O[C@H](CO[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3OC3OC[C@@H](O)[C@H](O)[C@H]3O)[C@H]2NC(C)=O)O[C@H](CO)[C@@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize