Taxonomic group: protista / Euglenozoa
(Phylum: Euglenozoa)
Host organism: (mammal)
Associated disease: Chagas disease [ICD11:
1F53 
, ICD11:
XN56V ];
infection due to Trypanosoma cruzi [ICD11:
XN56V ]
NCBI PubMed ID: 23430107Publication DOI: 10.1007/s10719-013-9469-7Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: luciamp
biof.ufrj.br
Institutions: Laboratório de Glicobiologia, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, 21 941 902, Ilha do Fundão, Cidade Universitária, Rio de Janeiro, RJ, Brazil
Trypanosoma cruzi, an intracellular protozoan etiologic agent of Chagas disease is covered by a dense coat of mucin-type glycoproteins, which is important to promote the parasite entry and persistence in the mammalian host cells. The O-glycosylation of T. cruzi mucins (Tc-mucins) is initiated by enzymatic addition of α-O-N-acetylglucosamine (GlcNAc) to threonine (Thr) by the UDP-GlcNAc:polypeptide α-N-acetylglucosaminyltransferase (pp-α-GlcNAcT) in the Golgi. The Tc-mucin is characterized by the presence of a high structural diversity of O-linked oligosaccharides found among different parasite strains, comprising two O-glycan Cores. In the Core 1, from strains principally associated with the domestic transmission cycle of Chagas disease, the GlcNAc O-4 is substituted with a β-galactopyranose (βGalp) unit, and in the most complex oligosaccharides the GlcNAc O-6 is further processed by the addition of β1→2-linked Galp residues creating a short linear Galp-containing chain. In the Core 2 structures, expressed by strains isolated from T. cruzi sylvatic hosts, the GlcNAc O-4 carries a β-galactofuranose (βGalf) unit and the GlcNAc O-6 can carry a branched Galpβ1→3[Galpβ1→2]Galpβ1→6 motif. The O-glycans carrying nonreducing terminal βGalp are available for sialylation by a surface T. cruzi trans-sialidase activity. Based on structural results, this review summarizes available data on the highly conserved process, which adds the GlcNAc unit in α-linkage to Thr residues the basis of the post-translational modification system in T. cruzi mucins. In addition, a mechanism unique employed by the parasite to transfer exogenous sialic acid residues to Tc-mucins is presented.
glycoproteins, Trypanosoma cruzi, mucins, trans-sialidase, pp-α-GlcNAcT, posttranslational modification
Structure type: oligomer
Location inside paper: p. 661, Fig.1
Trivial name: mucin-like glycan
Compound class: O-glycan
Contained glycoepitopes: IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_141794,IEDB_141807,IEDB_151531,IEDB_190606,IEDB_241097,SB_165,SB_166,SB_187,SB_195,SB_30,SB_7,SB_88
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 5693,
353153
Show glycosyltransferases
There is only one chemically distinct structure:
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