Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 30013106Publication DOI: 10.1038/s41467-018-05199-0Journal NLM ID: 101528555Publisher: London: Nature Publishing Group
Correspondence: Wang T <tuowang
lsu.edu>
Institutions: Complex Carbohydrate Research Center, University of Georgia, Athens, USA, Department of Chemistry, Louisiana State University, Baton Rouge, USA, Departments of Pediatrics, and Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center, New Orleans, USA, National High Magnetic Field Laboratory, Tallahassee, USA
The high mortality of invasive fungal infections, and the limited number and inefficacy of antifungals necessitate the development of new agents with novel mechanisms and targets. The fungal cell wall is a promising target as it contains polysaccharides absent in humans, however, its molecular structure remains elusive. Here we report the architecture of the cell walls in the pathogenic fungus Aspergillus fumigatus. Solid-state NMR spectroscopy, assisted by dynamic nuclear polarization and glycosyl linkage analysis, reveals that chitin and α-1,3-glucan build a hydrophobic scaffold that is surrounded by a hydrated matrix of diversely linked β-glucans and capped by a dynamic layer of glycoproteins and α-1,3-glucan. The two-domain distribution of α-1,3-glucans signifies the dual functions of this molecule: contributing to cell wall rigidity and fungal virulence. This study provides a high-resolution model of fungal cell walls and serves as the basis for assessing drug response to promote the development of wall-targeted antifungals
cell wall, cell wall polymers, fungi, solid-state NMR
Structure type: structural motif or average structure
Location inside paper: Fig. 1(c), STable 2
Trivial name: chitin
Compound class: cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Methods: GC-MS, composition analysis, ssNMR, TFA hydrolysis, MAS-DNP
Comments, role: forms hydrophobic core with α-glucan
3D data: conformation data; was identified in 11 polymorph types; intermolecular interactions between chitin and α-glucan and other glucans influence folding
Related record ID(s): 48634, 48636, 48650, 48651, 48652, 48689, 48691, 48694, 48715, 48752, 48757, 48764, 48770, 48771, 48772, 48773, 48774, 48775, 48785, 48794, 48795, 48801, 48804, 48828, 48853, 48859, 48872, 48900, 48901, 48902, 48984
NCBI Taxonomy refs (TaxIDs): 746128Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
NMR conditions: at 290(C) K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
2 Ac 174.8 22.6
bDGlcpN 103.6 55.0 72.9 83.0 75.7 60.9
1H NMR data:
missing...
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 2 | Ac | 174.8 | 22.6 | |
| | bDGlcpN | 103.6 | 55.0 | 72.9 | 83.0 | 75.7 | 60.9 |
|
There is only one chemically distinct structure:
Found 
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