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Taxonomic group: protista / Apicomplexa (Phylum: Apicomplexa)
Host organism: Homo sapiens
Associated disease: malaria due to Plasmodium falciparum [ICD11: 1F40

, ICD11: XN69B

]

NCBI PubMed ID: 26520586
Publication DOI: 10.1186/s12936-015-0949-z
Journal NLM ID: 101139802
Publisher: London: BioMed Central
Correspondence: tks1

st-andrews.ac.uk; luis.izquierdo

isglobal.org
Institutions: ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clinic, Universitat de Barcelona, Barcelona, Spain, Instituto de Medicina Molecular, Faculdade de Medicina da Universidade de Lisboa, Av. Prof. Egas Moniz, Edificio Egas Moniz, 1649-028, Lisbon, Portugal, Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife, KY16 9ST, UK

Glycoconjugates are important mediators of host-pathogen interactions and are usually very abundant in the surface of many protozoan parasites. However, in the particular case of Plasmodium species, previous works show that glycosylphosphatidylinositol anchor modifications, and to an unknown extent, a severely truncated N-glycosylation are the only glycosylation processes taking place in the parasite. Nevertheless, a detailed analysis of the parasite genome and the recent identification of the sugar nucleotide precursors biosynthesized by Plasmodium falciparum support a picture in which several overlooked, albeit not very prominent glycosylations may be occurring during the parasite life cycle. In this work, the authors review recent developments in the characterization of the biosynthesis of glycosylation precursors in the parasite, focusing on the outline of the possible fates of these precursors.

glycobiology, Plasmodium falciparum, Malaria

Structure type: oligomer
Location inside paper: p.427-2, Fig.2, Fig. 3
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

Comments, role: review

NCBI Taxonomy refs (TaxIDs): 5833
Show glycosyltransferases

There is only one chemically distinct structure:

[1*]OCC(COP(=O)(O)O[C@@H]1[C@@H](O[C@H]2O[C@H](CO)[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]4O[C@H](COP(=O)(O)OCCN[2*])[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](O)[C@H](O)[C@@H]3O)[C@H](O)[C@H]2N)[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O[1*])O[1*]

SVG MW SMILES 3D mol Ionize

R1 = LIP
R2 = protein