Taxonomic group: protista / Apicomplexa
(Phylum: Apicomplexa)
Host organism: Homo sapiens
Associated disease: malaria due to Plasmodium falciparum [ICD11:
1F40 
, ICD11:
XN69B ]
NCBI PubMed ID: 21225189Publication DOI: 10.1590/s0074-02762010000800001Journal NLM ID: 7502619Publisher: Rio de Janeiro: Instituto Oswaldo Cruz
Correspondence: luciamp
biof.ufrj.br
Institutions: Instituto de Biofísica Carlos Chagas Filho, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil, Institut fur Virologie, Universitat Marburg, Marburg, Germany and Unité de Glycobiologie Structurale et Fonctionnelle, Universite des Sciences et Technologies de Lille, Villeneuve-d'Ascq, France
Human malignant malaria is caused by Plasmodium falciparum and accounts for almost 900,000 deaths per year, the majority of which are children and pregnant women in developing countries. There has been significant effort to understand the biology of P. falciparum and its interactions with the host. However, these studies are hindered because several aspects of parasite biology remain controversial, such as N- and O-glycosylation. This review describes work that has been done to elucidate protein glycosylation in P. falciparum and it focuses on describing biochemical evidence for N- and O-glycosylation. Although there has been significant work in this field, these aspects of parasite biochemistry need to be explored further.
glycosylation, glycoproteins, O-glycan, Plasmodium, N-glycan
Structure type: monomer
Location inside paper: p. 953
Aglycon: Ser/Thr-peptide
Compound class: O-glycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_150900,IEDB_151531
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 5833
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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