Taxonomic group: protista / Apicomplexa
(Phylum: Apicomplexa)
Associated disease: malaria due to Plasmodium falciparum [ICD11:
1F40 
, ICD11:
XN69B ]
NCBI PubMed ID: 38262838Publication DOI: 10.1016/j.pt.2023.12.006Journal NLM ID: 100966034Publisher: Oxford, UK: Elsevier Science
Correspondence: Gowda DC <Channe.gowda
nih.gov>; Miller LH <louis.miller
nih.gov>
Institutions: Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, Rockville, MD, USA, Department of Biochemistry and Molecular Biology, The Pennsylvania State University College of Medicine, Milton S. Hershey Medical Center, Hershey, PA, USA
In malaria parasites, although post-translational modification of proteins with N-. O-, and C-glycosidic bond-linked glycans is limited, it is confined to relatively fewer proteins in which the glycans are present at significant levels and may have important functions. Furthermore, several proteins are modified with glycosylphosphatidylinositols (GPIs) which represent the predominant glycan synthesized by parasites. Modification of proteins with GPIs is obligatory for parasite survival as GPI-anchored proteins (GPI-APs) play essential roles in all life cycle stages of the parasites, including development, egress, gametogenesis, motility, and host cell adhesion and invasion. Here, we discuss the current knowledge on the structures and potential functions of the glycan moieties of parasite proteins. The knowledge has important implications for the development of drugs and vaccines for malaria
glycosylation, Malaria, Plasmodium parasites, glycan structure and function
Structure type: oligomer
Location inside paper: pg. 135, Fig. 2, B, structure 5
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_983930,SB_198,SB_44,SB_67,SB_72
Comments, role: review
Related record ID(s): 15636, 15637, 15638, 15639, 15640, 15642
NCBI Taxonomy refs (TaxIDs): 5833
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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