Taxonomic group: protista / Evosea
(Phylum: Evosea)
Organ / tissue: Life stage: trophozoiteAssociated disease: intestinal infections due to Entamoeba [ICD11:
1A36.0 
, ICD11:
XN3S1 ];
amoebic liver abscess [ICD11:
1A36.10 , ICD11:
XN3S1 ];
infection due to Entamoeba histolytica [ICD11:
XN82F ]
The structure was elucidated in this paperNCBI PubMed ID: 30444974Publication DOI: 10.1016/j.exppara.2018.11.003Journal NLM ID: 0370713Publisher: Orlando, FL : Academic Press
Correspondence: Maria S. Flores <maria.floresgz
uanl.edu.mx>; <floresgms
yahoo.com>
Institutions: Universidad Autónoma de Nuevo León, Facultad de Ciencias Biológicas, Instituto de Biotecnología, San Nicolás de los Garza, Nuevo León, Mexico, Department of Head and Neck Surgery, University of Texas MD Anderson Cancer Center, Houston, Texas, USA
Entamoeba histolytica harbors an extensive intracellular distribution of ubiquitin-proteasome systems important for numerous cellular processes. However, glycosylation studies of ubiquitin-proteasome components have not yet been elucidated. Here we report the partial characterization of N-linked glycosylation profile in E. histolytica ubiquitin by Fluorophore-Assisted Carbohydrate Electrophoresis (FACE), Nanoelectrospray Ionization-Tandem Mass Spectrometry (NSI-MS), Matrix-Assisted Laser-Desorption time-of-flight Mass Spectrometry (MALDI-TOF MS) and Gas Chromatography-Mass Spectrometry (GC-MS) analysis. To our knowledge, the data presented in this report represents the first structural glycomics analysis of E. histolytica ubiquitin, while most of the reports are performed on whole parasitic glycan profiles. The glycan profile of E. histolytica ubiquitin has high mannose N-glycan structures. The N-linked glycan profile showed fragments from Hex3HexNAc2 to Hex9HexNAc2. Based in our findings and ubiquitin function, we hypothesize that the same ubiquitin Asn-Asp-Ser sequon carries heterogenic glycosylations, at different metabolic pathway stages according to ubiquitin functional requirements. Finally, we propose a set of possible high mannose N-glycan structures that will help to elucidate the ubiquitin biochemical composition and may well represent good targets for anti-amoebic drugs.
MALDI-TOF MS, Entamoeba histolytica, N-glycosylation, GC-MS, N-glycans, Ubiquitin, Continuous elution electrophoresis, NSI-MS/MS
Structure type: structural motif or average structure ; 1376 [M+Na]+
Location inside paper: p. 43, Fig. 7, Hex4GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_143632,IEDB_144983,IEDB_144995,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_164479,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85
Methods: GC-MS, SDS-PAGE, MALDI-TOF MS, nESI-CID-MS, FACE, enzymatic digestion, permethylation, hydrazinolysis, nESI-MS/MS
Comments, role: N-glycans in the ubiquitin glycoprotein
Related record ID(s): 7356, 8274, 8275, 8276, 8277, 8278, 8279
NCBI Taxonomy refs (TaxIDs): 294381
Show glycosyltransferases
There is only one chemically distinct structure:
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