Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Associated disease: infection due to Candida albicans [ICD11: XN31P]
The structure was elucidated in this paperNCBI PubMed ID: 37520856Publication DOI: 10.1016/j.tcsw.2023.100109Journal NLM ID: 101728565Publisher: Amsterdam: Elsevier
Correspondence: A. Ardá <aarda
cicbiogune.es>; J. Jiménez-Barbero <jjbarbero
cicbiogune.es>; N.E. Nifantiev <nen
ioc.ac.ru>
Institutions: Laboratory of Glycoconjugate Chemistry, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, CIC bioGUNE, Basque Research Technology Alliance, BRTA, 48160 Derio, Spain, Medical Research Council Centre for Medical Mycology, University of Exeter, Exeter EX4 4QD, United Kingdom, IKERBASQUE, Basque Foundation for Science and Technology, Euskadi Plaza 5, 48009 Bilbao, Spain, Department of Organic & Inorganic Chemistry, Faculty of Science and Technology, University of the Basque Country, 48940 Leioa, Spain
The dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) is an innate immune C-type lectin receptor that recognizes carbohydrate-based pathogen associated with molecular patterns of various bacteria, fungi, viruses and protozoa. Although a range of highly mannosylated glycoproteins have been shown to induce signaling via DC-SIGN, precise structure of the recognized oligosaccharide epitope is still unclear. Using the array of oligosaccharides related to selected fragments of main fungal antigenic polysaccharides we revealed a highly specific pentamannoside ligand of DC-SIGN, consisting of α-(1→2)-linked mannose chains with one inner α-(1→3)-linked unit. This structural motif is present in Candida albicans cell wall mannan and corresponds to its antigenic factors 4 and 13b. This epitope is not ubiquitous in other yeast species and may account for the species-specific nature of fungal recognition via DC-SIGN. The discovered highly specific oligosaccharide ligands of DC-SIGN are tractable tools for interdisciplinary investigations of mechanisms of fungal innate immunity and anti-Candida defense. Ligand- and receptor-based NMR data demonstrated the pentasaccharide-to-DC-SIGN interaction in solution and enabled the deciphering of the interaction topology.
DC-SIGN, glycoarray, Candida albicans mannan, NMR binding and conformational studies, oligomannoside ligand
Structure type: oligomer
Location inside paper: Fig. 5(a), pentasaccharide 29
Aglycon: (CH2)3NH2, linker-biotin
Trivial name: cell wall mannan
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72
Methods: NMR, MD simulations, NOESY, conformational analysis, 1H STD NMR, glycoarray
Biological activity: Pentamannoside is structurally related to the antigenic factors 4 and 13b, is a key epitope that is specifically and efficiently recognized by the immune cell receptor DC-SIGN.
Synthetic data: chemical
3D data: model building for the DC-SIGN lectin and complexes
Related record ID(s): 41050
NCBI Taxonomy refs (TaxIDs): 5476
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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