Show legend Show as text

Structure type: oligomer
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 1735
  McConville MJ, Ferguson MAJ "The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes" - Biochemical Journal 294 (1993) 305-324
  

  No abstract available

  NCBI PubMed ID: 8373346
  Publication DOI: 10.1042/bj2940305
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Institutions: Department of Biochemistry, University of Dundee, U.K., Department of Biochemistry, University of Dundee, U.K
  
   
  
  Trypanosoma brucei
  CSDB ID 106315 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoproteins (VSG)
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5893
  Barreto-Bergter E, Vermelho AB "Structures of glycolipids found in trypanosomatids: Contribution to parasite functions" - The Open Parasitology Journal 4 (2010) 84-97
  

  Neutral monohexosylceramides (CMHs) globosides (globotriasyl ceramides), other glycosphingolipids (GSLs) and more complex structures such as glycoinositol-phospholipids(GIPLs) and glycosyl phosphatidylinositol (GPI) anchors have been described in several members of the trypanosomatid family. These highly bioactive molecules are not only components of biological structures but also participants in host-parasite interactions such as macrophage invasion, antigenic presentation and signal transduction. Glycolipid structures have been studied using mass spectrometry (MS).This review describes a wide range of glycoconjugates with unique and complex structures that are present in several trypanosomatid species. Their structures are described in the context of their biological significance.

  mass spectrometry, GIPLs, GPI-anchor proteins, GSLs, Trypanosomatids

  Publication DOI: 10.2174/1874421401004010084
  Journal NLM ID: 101552240
  Publisher: Hilversum: Bentham Science Publishers
  Correspondence: eliana.bergter@micro.ufrj.br
  Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes (IMPPG), Centro de Ciências da Saúde (CCS) Universidade Federal do Rio de Janeiro (UFRJ), Bloco I, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
  
   
  
  Trypanosoma brucei
  CSDB ID 5492 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoproteins (VSG)
Compound class: glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5904
  Chiodi CG, Verli H "Structural characterization of NETNES glycopeptide from Trypanosoma cruzi" - Carbohydrate Research 373 (2013) 28-34
  

  Trypanosoma cruzi is a protozoan, responsible for Chagas disease, that parasites triatomines and some vertebrates, mainly Homo sapiens. In 2010, nearly 10 million people in whole world, most from Latin America, had Chagas disease, which is an illness of high morbidity, low mortality, and serious problems of quality of life. The available treatment has high toxicity and low efficacy at chronic phase. Some of the protozoan antigenic or virulence factors include complex carbohydrate structures that, due to their uniqueness, may constitute potential selective targets for the development of new treatments. One example of such structures is NETNES, a low abundance T. cruzi glycopeptide, comprising 13 amino acid residues, one or two N-glycosylation chains, a GPI anchor and two P-glycosylations. In this context, the current work aims to obtain an atomic model for NETNES, including its glycan chains and membrane attachment, in order to contribute in the characterization of its structure and dynamics. Based on POPC and GPI models built in agreement with experimental data, our results indicate that, in the first third of the simulation, NETNES peptide is very flexible in solution, bending itself between asparagine residues and lying down on some carbohydrates and membrane, exposing amino acid residues and some other glycans, mainly terminal mannoses, to the extracellular medium, remaining in this position until the end of simulations.

  molecular dynamics, glycopeptide, Trypanosoma cruzi, N-glycosylation, GPI anchor, NETNES

  NCBI PubMed ID: 23578542
  Publication DOI: 10.1016/j.carres.2013.03.010
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: H. Verli
  Institutions: Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre 91500-970, RS, Brazil
  Methods: conformation analysis, MD simulations, topological information
  
   
  
  Trypanosoma brucei
  CSDB ID 4839 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5908
  Cortes LK, Scarcelli JJ, Taron CH "Complementation of essential yeast GPI mannosyltransferase mutations suggests a novel specificity for certain Trypanosoma and Plasmodium PigB proteins" - PLoS One 9(1) (2014) e87673
  

  The glycosylphosphatidylinositol (GPI) anchor is an essential glycolipid that tethers certain eukaryotic proteins to the cell surface. The core structure of the GPI anchor is remarkably well conserved across evolution and consists of NH2-CH2-CH2-PO4-6Manα1,2Manα1,6Manα1,4-GlcNα1,6-myo-inositol-PO4-lipid. The glycan portion of this structure may be modified with various side-branching sugars or other compounds that are heterogeneous and differ from organism to organism. One such modification is an α(1,2)-linked fourth mannose (Man-IV) that is side-branched to the third mannose (Man-III) of the trimannosyl core. In fungi and mammals, addition of Man-III and Man-IV occurs by two distinct Family 22 α(1,2)-mannosyltransferases, Gpi10/PigB and Smp3/PigZ, respectively. However, in the five protozoan parasite genomes we examined, no genes encoding Smp3/PigZ proteins were observed, despite reports of tetramannosyl-GPI structures (Man4-GPIs) being produced by some parasites. In this study, we tested the hypothesis that the Gpi10/PigB proteins produced by protozoan parasites have the ability to add both Man-III and Man-IV to GPI precursors. We used yeast genetics to test the in vivo specificity of Gpi10/PigB proteins from several Plasmodium and Trypanosoma species by examining their ability to restore viability to Saccharomyces cerevisiae strains harboring lethal defects in Man-III (gpi10Δ) or Man-IV (smp3Δ) addition to GPI precursor lipids. We demonstrate that genes encoding PigB enzymes from T. cruzi, T. congolense and P. falciparum are each capable of separately complementing essential gpi10Δ and smp3Δ mutations, while PIGB genes from T. vivax and T. brucei only complement gpi10Δ. Additionally, we show the ability of T. cruzi PIGB to robustly complement a gpi10Δ/smp3Δ double mutant. Our data suggest that certain Plasmodium and Trypanosoma PigB mannosyltransferases can transfer more than one mannose to GPI precursors in vivo, and suggest a novel biosynthetic mechanism by which Man4-GPIs may be synthesized in these organisms.

  glycan, Glycosylphosphatidylinositol, Mannosyltransferase, Plasmodium, GPI, protozoan, Trypanosoma, Saccharomyces cerevisiae

  NCBI PubMed ID: 24489949
  Publication DOI: 10.1371/journal.pone.0087673
  Journal NLM ID: 101285081
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: taron@neb.com
  Institutions: New England Biolabs, Ipswich, Massachusetts, United States of America, New England Biolabs, Ipswich, USA
  Methods: PCR, genetic methods, BLASTp
  
   
  
  Trypanosoma brucei
  CSDB ID 7278 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoproteins (VSG) GPI anchor, variant surface glycoproteins (VSG) GPI-anchor
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5910
  Cummings RD, Van Die I "Parasitic Infections" - Book: In: Essentials of Glycobiology [Internet]. 3rd edition. (2017)
  

  Parasitic protozoans and helminths (worms) synthesize glycans with structures often different from those typically found in vertebrates and are typically antigenic. Parasites also express glycan-binding proteins (GBPs) involved in host invasion and parasitism. As part of the disease process, parasite glycans can trigger the host's innate immune system, which can lead to the induction of adaptive immune responses. This chapter discusses the major roles of glycoconjugates in parasitic infections.

  NCBI PubMed ID: 28876851
  Publication DOI: 10.1101/glycobiology.3e.043
  Publisher: Cold Spring Harbor (NY), Cold Spring Harbor Laboratory Press, 2015-2017
  Correspondence: Richard D. Cummings ; Irma van Die
  Editors: Varki A, Cummings RD, Esko JD
  Institutions: Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA, Department of Molecular Cell Biology & Immunology, VU University Center, Amsterdam, The Netherlands
  
   
  
  Trypanosoma brucei
  CSDB ID 7280 (all data & tools)
• Article ID: 6349
  Cummings RD, Hokke CH, Haslam SM "Parasitic Infections" - Book: Essentials of Glycobiology [Internet]. 4rd edition (2022)
  

  Parasitic protozoans and helminths (worms) synthesize glycans with structures often different from those typically found in vertebrates, and are thus often antigenic. Parasites also express glycan-binding proteins (GBPs) involved in host invasion and parasitism. As part of the disease process, parasite glycans can trigger the host's innate immune system, which can lead to the induction of adaptive immune responses. This chapter discusses the major roles of glycoconjugates in parasitic infections.

  NCBI PubMed ID: 35536961
  Publication DOI: 10.1101/glycobiology.4e.43
  Publisher: Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
  Correspondence: R.D. Cummings
  Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger RH
  Institutions: Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA, Department of Molecular Cell Biology & Immunology, VU University Center, Amsterdam, The Netherlands
  
   
  
  Trypanosoma brucei
  CSDB ID 10472 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 956 [M+2H]2+
Trivial name: sVSG, soluble-form VSG
Compound class: GPI-anchor VSG
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_140425,IEDB_140426,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_145015,IEDB_150900,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5917
  Denton H, Fyffe S, Smith TK "GDP-mannose pyrophosphorylase is essential in the bloodstream form of Trypanosoma brucei" - Biochemical Journal 425(3) (2010) 603-614
  

  A putative GDP-Man PP (guanidine diphosphomannose pyrophosphorylase) gene from Trypanosoma brucei (TbGDP-Man PP) was identified in the genome and subsequently cloned, sequenced and recombinantly expressed, and shown to be a catalytically active dimer. Kinetic analysis revealed a Vmax of 0.34 μmol/min per mg of protein and Km values of 67 μM and 12 μM for GTP and mannose 1-phosphate respectively. Further kinetic studies showed GDP-Man was a potent product feedback inhibitor. RNAi (RNA interference) of the cytosolic TbGDP-Man PP showed that mRNA levels were reduced to ~20% of wild-type levels, causing the cells to die after 3-4 days, demonstrating that TbGDP-Man PP is essential in the bloodstream form of T. brucei and thus a potential drug target. The RNAi-induced parasites have a greatly reduced capability to form GDP-Man, leading ultimately to a reduction in their ability to synthesize their essential GPI (glycosylphosphatidylinositol) anchors. The RNAi-induced parasites also showed aberrant N-glycosylation of their major cell-surface glycoprotein, variant surface glycoprotein, with loss of the high-mannose Man9GlcNAc2 N-glycosylation at Asn428 and formation of complex N-glycans at Asn263.

  Glycosylphosphatidylinositol, N-glycosylation, Trypanosoma brucei, variant surface glycoprotein, essentiality, guanidine diphosphomannose pyrophosphorylase

  NCBI PubMed ID: 19919534
  Publication DOI: 10.1042/BJ20090896
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Correspondence: tks1@st-andrews.ac.uk
  Institutions: Biomolecular Sciences Research Complex, The North Haugh, The University, St Andrews, Fife KY16 9ST, Scotland, UK
  Methods: gel filtration, ESI-MS, ESI-MS/MS, genetic methods, HPLC, enzymatic digestion, Southern blotting, RT-PCR, HPTLC, cloning, enzymatic assay
  
   
  
  Trypanosoma brucei 427 variant 221
  CSDB ID 4868 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5918
  Dettmann R, Ziegler T "Synthesis of octyl S-glycosides of tri- to pentasaccharide fragments related to the GPI anchor of Trypanosoma brucei" - Carbohydrate Research 346(15) (2011) 2348-2361
  

  The three oligosaccharide octyl-S-glycosides Man-α1,6-Man-α1,4-GlcNH(2)-α1,S-Octyl (19), Man-α1,6-(Gal-α1,3)Man-α1,4-GlcNH(2)-α1,S-Octyl (27) and Man-α1,2-Man-α1,6-(Gal-α1,3)Man-α1,4-GlcNH(2)-α1,S-Octyl (37), related to the GPI anchor of Trypanosoma brucei were prepared by a stepwise and block-wise approach from octyl 2-azido-2-deoxy-3,6-di-O-benzyl-1-thio-α-D-glucopyranoside (8) and octyl 2-O-benzoyl-4,6-O-(1,1,3,3-tetraisopropyl-1,3-disiloxane-1,3-diyl)-1-thio-α-D-mannopyransoside (9). Glucosamine derivative 8 was obtained from 1,3,4,6-tetra-O-acetyl-2-azido-2-desoxy-β-D-glucopyranose (1) in five steps. Mannoside 9 was converted into the corresponding imidate 12 and coupled with 8 to give disaccharide octyl-S-glycoside 13 which was further mannosylated to afford trisaccharide 19 upon deprotection. Likewise, mannoside 9 was galactosylated, converted into the corresponding imidate and coupled with 8 to give trisaccharide 25. Mannosylation of the latter afforded tetrasaccharide 27 upon deprotection. Condensation of 25 with disaccharide imidate 35 gave, upon deprotection of the intermediates, the corresponding pentasaccharide octyl-S-glycoside 37. Saccharides 19, 27 and 37 are suitable substrates for studying the enzymatic glycosylation pattern of the GPI anchor of T. brucei.

  glycosylation, Trypanosoma brucei, GPI anchor, Glycodesilylation

  NCBI PubMed ID: 21920515
  Publication DOI: 10.1016/j.carres.2011.08.001
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: T. Ziegler
  Institutions: Institute of Organic Chemistry, University of Tuebingen, Auf der Morgenstelle 18, 72076 Tuebingen, Germany
  Methods: 13C NMR, 1H NMR, TLC, chemical synthesis, chemical methods, MALDI-TOF MS
  
   
  
  Trypanosoma brucei 427 variant 221
  CSDB ID 7288 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: -Asn-XSer/Thr-
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_742246,IEDB_918313,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72,SB_87,SB_88

• Article ID: 5919
  Duncan SM, Nagar R, Damerow M, Yashunsky DV, Bruzzi B, Nikolaev AV, Ferguson MAJ "A Trypanosoma brucei β3 glycosyltransferase superfamily gene encodes a β1-6 GlcNAc-transferase mediating N-glycan and GPI anchor modification" - Journal of Biological Chemistry 294(4) (2021) 101153
  

  The parasite Trypanosoma brucei exists in both a bloodstream form (BSF) and a procyclic form (PCF), which exhibit large carbohydrate extensions on the N-linked glycans and glycosylphosphatidylinositol (GPI) anchors, respectively. The parasite's glycoconjugate repertoire suggests at least 38 glycosyltransferase (GT) activities, 16 of which are currently uncharacterized. Here, we probe the function(s) of the uncharacterized GT67 glycosyltransferase family and a β3 glycosyltransferase (β3GT) superfamily gene, TbGT10. A BSF-null mutant, created by applying the diCre/loxP method in T. brucei for the first time, showed a fitness cost but was viable in vitro and in vivo and could differentiate into the PCF, demonstrating nonessentiality of TbGT10. The absence of TbGT10 impaired the elaboration of N-glycans and GPI anchor side chains in BSF and PCF parasites, respectively. Glycosylation defects included reduced BSF glycoprotein binding to the lectin ricin and monoclonal antibodies mAb139 and mAbCB1. The latter bind a carbohydrate epitope present on lysosomal glycoprotein p67 that we show here consists of (-6Galβ1-4GlcNAcβ1-)≥4 poly-N-acetyllactosamine repeats. Methylation linkage analysis of Pronase-digested glycopeptides isolated from BSF wild-type and TbGT10 null parasites showed a reduction in 6-O-substituted- and 3,6-di-O-substituted-Gal residues. These data define TbGT10 as a UDP-GlcNAc:βGal β1-6 GlcNAc-transferase. The dual role of TbGT10 in BSF N-glycan and PCF GPI-glycan elaboration is notable, and the β1-6 specificity of a β3GT superfamily gene product is unprecedented. The similar activities of trypanosome TbGT10 and higher-eukaryote I-branching enzyme (EC 2.4.1.150), which belong to glycosyltransferase families GT67 and GT14, respectively, in elaborating N-linked glycans, are a novel example of convergent evolution.

  N-acetylglucosaminyltransferase, Glycosylphosphatidylinositol, N-glycosylation, GPI, N-glycan, Trypanosoma brucei glycosyltransferase

  NCBI PubMed ID: 34478712
  Publication DOI: 10.1016/j.jbc.2021.101153
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: m.a.j.ferguson@dundee.ac.uk
  Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom
  Methods: methylation, PCR, GC-MS, DNA techniques, Western blotting, genetic methods, enzymatic digestion, conjugation, lectin blotting, biolayer interferometry (BLI) measurements
  
   
  
  Trypanosoma brucei
  CSDB ID 4886 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoproteins (VSG) GPI 221
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 5932
  Fujita M, Kinoshita T "Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins" - FEBS Letters 584(9) (2010) 1670-1677
  

  Glycosylphosphatidylinositol (GPI) anchoring of proteins is a conserved post-translational modification in eukaryotes. In mammalian cells, approximately 150 proteins on the plasma membrane are attached to the cell surface by GPI anchors, which confer specific properties on proteins, such as association with membrane microdomains. The structures of lipid and glycan moieties on GPI anchors are remodeled during biosynthesis and after attachment to proteins. The remodeling processes are critical for transport and microdomain-association of GPI-anchored proteins. Here, we describe the structural remodeling of GPI anchors and genes required for the processes in mammals, yeast, and trypanosomes.

  Glycosylphosphatidylinositol, Lipid raft, endoplasmic reticulum (ER), Golji, microdomain, remodeling

  NCBI PubMed ID: 19883648
  Publication DOI: 10.1016/j.febslet.2009.10.079
  Journal NLM ID: 0155157
  Publisher: Elsevier
  Correspondence: T. Kinoshita
  Institutions: Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan
  
   
  
  Trypanosoma brucei
  CSDB ID 7301 (all data & tools)
• Article ID: 5938
  Grube M, Lee BY, Gard M, Michel D, Vilotijevic I, Malik A, Seeberger PH, Silva DV "Synthesis of Galactosylated Glycosylphosphatidylinositol Derivatives from Trypanosoma brucei" - Chemistry: a European Journal 24(13) (2018) 3271-3282
  

  Trypanosoma brucei uses variant surface glycoproteins (VSGs) to evade the host immune system and ensure parasitic longevity in animals and humans. VSGs are attached to the cell membrane by complex glycosylphosphatidylinositol anchors (GPI). Distinguishing structural feature of VSG GPIs are multiple α- and β-galactosides attached to the conserved GPI core structure. T. brucei GPIs have been associated with macrophage activation and alleviation of parasitemia during infection, acting as disease onset delaying antigens. Literature reports that link structural modifications in the GPIs to changes in biological activity are contradictory. We have established a synthetic route to prepare structurally overlapping GPI derivatives bearing different T. brucei characteristic structural modifications. The GPI collection will be used to assess the effect of galactosylation and phosphorylation on T. brucei GPI immunomodulatory activity, and to perform an epitope mapping of this complex glycolipid as potential diagnostic marker for Trypanosomiasis. A strategy for the synthesis of a complete α-tetragalactoside using the 2-naphthylmethyl protecting group and for subsequent attachment of GPI fragments to peptides is presented.

  carbohydrates, glycolipid, Glycosylphosphatidylinositol, Trypanosoma brucei, GPI synthesis

  NCBI PubMed ID: 29314341
  Publication DOI: 10.1002/chem.201705511
  Journal NLM ID: 9513783
  Publisher: Weinheim: VCH Verlagsgesellschaft/Verlag I
  Correspondence: daniel.varon@mpikg.mpg.de
  Institutions: Biomolecular Systems Department, Max-Planck-Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476, Potsdam, Germany, Department of Biology, Chemistry and Pharmacy, Free University Berlin, Arnimallee 22, 14195, Berlin, Germany, Science for Life Laboratory, Tomtebodavagen 23A, 17121, Stockholm, Sweden, Institute of Organic Chemistry and Macromolecular Chemistry, Friedrich-Schiller-University Jena, Humboldtstr. 10, Office 310A, 07743, Jena, Germany
  Methods: 13C NMR, 1H NMR, NMR-2D, TLC, ESI-MS, chemical synthesis, HPLC, HPAEC-PAD, column chromatography
  
   
  
  Trypanosoma brucei
  CSDB ID 7307 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GPI-anchor, variant surface glycoproteins (VSG)
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 5943
  Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" - Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
  

  This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.

  O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation

  Publication DOI: 10.1016/B978-0-12-374546-0.00012-2
  Publisher: Amsterdam: Elsevier
  Correspondence: malcolmm@unimelb.edu.au
  Editors: Moran A
  Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
  
   
  
  Trypanosoma brucei
  CSDB ID 7312 (all data & tools)
• Article ID: 6350
  de Lederkremer RM, Giorgi ME, Marino C "The α-Galactosyl Carbohydrate Epitope in Pathogenic Protozoa" - ACS Infectious Diseases 8(11) (2022) 2207-2222
  

  The α-gal epitope, which refers to the carbohydrate α-D-Galp-(1→3)-β-D-Galp-(1→4)-D-GlcNAc-R, was first described in the glycoconjugates of mammals other than humans. Evolution caused a mutation that resulted in the inactivation of the α-1,3-galactosyltransferase gene. For that reason, humans produce antibodies against α-D-Galp containing glycoproteins and glycolipids of other species. We summarize here the glycoconjugates with α-D-Galp structures in Trypanosoma, Leishmania, and Plasmodium pathogenic protozoa. These were identified in infective stages of Trypanosoma cruzi and in Plasmodium sporozoites. In Leishmania, α-D-Galp is linked differently in the glycans of glycoinositolphospholipids (GIPLs). Chemically synthesized neoglycoconjugates have been proposed as diagnostic tools and as antigens for vaccines. Several syntheses reported for the α-gal trisaccharide, also called the Galili epitope, and the glycans of GIPLs found in Leishmania, the preparation of neoglycoconjugates, and the studies in which they were involved are also included in this Review.

  leishmania, Plasmodium, mucins, Trypanosoma, α-galactosyl, anti-α-Gal antibodies

  NCBI PubMed ID: 36083842
  Publication DOI: 10.1021/acsinfecdis.2c00370
  Journal NLM ID: 101654580
  Publisher: Washington, DC: American Chemical Society
  Correspondence: R.M. de Lederkremer ; C. Marino
  Institutions: CIHIDECAR, Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón II, Ciudad Universitaria, 1428 Buenos Aires, Argentina
  
   
  
  Trypanosoma brucei
  CSDB ID 10489 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GPI glycan
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 5954
  Koeller CM, Tiengwe C, Schwartz KJ, Bangs JD "Steric constraints control processing of glycosylphosphatidylinositol anchors in Trypanosoma brucei" - Journal of Biological Chemistry 295(8) (2020) 2227-2238
  

  The transferrin receptor (TfR) of the bloodstream form (BSF) of Trypanosoma brucei is a heterodimer comprising glycosylphosphatidylinositol (GPI)-anchored expression site-associated gene 6 (ESAG6 or E6) and soluble ESAG7. Mature E6 has five N-glycans, consisting of three oligomannose and two unprocessed paucimannose structures. Its GPI anchor is modified by the addition of 4-6 α-galactose residues. TfR binds tomato lectin (TL), specific for N-acetyllactosamine (LacNAc) repeats, and previous studies have shown transport-dependent increases in E6 size consistent with post-glycan processing in the endoplasmic reticulum. Using pulse-chase radiolabeling, peptide-N-glycosidase F treatment, lectin pulldowns, and exoglycosidase treatment, we have now investigated TfR N-glycan and GPI processing. E6 increased ∼5 kDa during maturation, becoming reactive with both TL and Erythrina cristagalli lectin (ECL, terminal LacNAc), indicating synthesis of poly-LacNAc on paucimannose N-glycans. This processing was lost after exoglycosidase treatment and after RNAi-based silencing of TbSTT3A, the oligosaccharyltransferase that transfers paucimannose structures to nascent secretory polypeptides. These results contradict previous structural studies. Minor GPI processing was also observed, consistent with α-galactose addition. However, increasing the spacing between E6 protein and the GPI ω-site (aa 4-7) resulted in extensive post-translational processing of the GPI anchor to a form that was TL/ECL-reactive, suggesting the addition of LacNAc structures, confirmed by identical assays with BiPNHP, a non-N-glycosylated GPI-anchored reporter. We conclude that BSF trypanosomes can modify GPIs by generating structures reminiscent of those present in insect-stage trypanosomes and that steric constraints, not stage-specific expression of glycosyltransferases, regulate GPI processing.

  Trypanosome, N-linked glycosylation, glycobiology, Trypanosoma brucei, glycosylphosphatidylinositol (GPI anchor), glycosylphosphatidylinositol processing, kinetoplastid protozoa, N-glycan processing, transferrin, transferrin receptor

  NCBI PubMed ID: 31932305
  Publication DOI: 10.1074/jbc.RA119.010847
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: jdbangs@buffalo.edu
  Institutions: Department of Microbiology and Immunology, School of Medicine and Biomedical Sciences, University at Buffalo (SUNY), Buffalo, New York 14214, Department of Medical Microbiology and Immunology, University of Wisconsin, Madison, Wisconsin, 53706
  Methods: radiolabeling, serological methods, genetic methods, enzymatic digestion, RT-PCR, immunoprecipitation assay
  
   
  
  Trypanosoma brucei
  CSDB ID 7323 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: Asn419-protein
Trivial name: variant surface glycoprotein (VSG) MITat1.8
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_115013,IEDB_120354,IEDB_123890,IEDB_130645,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144987,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_742246,IEDB_918313,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_31,SB_44,SB_67,SB_7,SB_72,SB_87

• Article ID: 5963
  Mehlert A, Sullivan L, Ferguson MAJ "Glycotyping of Trypanosoma brucei variant surface glycoprotein MITat1.8" - Molecular and Biochemical Parasitology 174(1) (2010) 74-77
  

  Following a switch from variant surface glycoprotein MITat1.4 to variant surface glycoprotein MITat1.8 expression by Lister strain 427 Trypanosoma brucei brucei parasites, the latter uncharacterized variant surface glycoprotein was analysed. Variant surface glycoprotein MITat1.8 was found to be a disulphide-linked homodimer, containing a complex N-linked glycan at Asn58 and a glycosylphosphatidylinositol membrane anchor attached to Asp419. Mass spectrometric analyses demonstrated that the N-glycan is exclusively Galβ1-4GlcNAcβ1-2Manα1-3(Galβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAc and that the conserved Man3GlcN-myo-inositol glycosylphosphatidylinositol anchor glycan core is substituted with an average of 4 hexose, most likely galactose, residues. The presence of a complex N-glycan at Asn58 is consistent with the relatively acidic environment of the Asn58 N-glycosylation sequon, that predicts N-glycosylation by T. brucei oligosaccharyltransferase TbSTT3A with a Man5GlcNAc2 structure destined for processing to a paucimannose and/or complex N-glycan (Izquierdo L, Schulz B, Rodrigues JA et al. EMBO J 2009;28:2650–61 [12])

  mass spectrometry, Glycosylphosphatidylinositol, N-glycosylation, GPI, Trypanosoma brucei, N-linked oligosaccharides

  NCBI PubMed ID: 20558211
  Publication DOI: 10.1016/j.molbiopara.2010.06.007
  Journal NLM ID: 8006324
  Correspondence: M.A.J. Ferguson
  Institutions: Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom
  Methods: GC-MS, SDS-PAGE, ESI-MS, anion-exchange chromatography, Western blotting, MS/MS, MALDI-TOF MS, enzymatic digestion, HF treatment, permethylation, LC-MS
  
   
  
  Trypanosoma brucei 427, Trypanosoma brucei MITat1.8
  CSDB ID 8173 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoprotein (VSG) GPI anchor
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_115013,IEDB_120354,IEDB_123890,IEDB_130645,IEDB_130651,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141492,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_143632,IEDB_144983,IEDB_144987,IEDB_144993,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153201,IEDB_153220,IEDB_156489,IEDB_156493,IEDB_156494,IEDB_156557,IEDB_156983,IEDB_167072,IEDB_176772,IEDB_190606,IEDB_221845,IEDB_241097,IEDB_474450,IEDB_742245,IEDB_742246,IEDB_742247,IEDB_742248,IEDB_918313,IEDB_918314,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_31,SB_44,SB_62,SB_67,SB_7,SB_72,SB_87,SB_88

• Article ID: 5969
  Morotti AMM, Martins-Teixeira MB, Carvalho I "Protozoan Parasites Glycosylphosphatidylinositol Anchors: Structures, Functions and Trends for Drug Discovery" - Current Medicinal Chemistry 26(23) (2019) 4301-4322
  

  Background: Glycosylphosphatidylinositol (GPI) anchors are molecules located on cell membranes of all eukaryotic organisms. Proteins, enzymes, and other macromolecules which are anchored by GPIs are essential elements for interaction between cells, and are widely used by protozoan parasites when compared to higher eukaryotes. Methods: More than one hundred references were collected to obtain broad information about mammalian and protozoan parasites' GPI structures, biosynthetic pathways, functions and attempts to use these molecules as drug targets against parasitic diseases. Differences between GPI among species were compared and highlighted. Strategies for drug discovery and development against protozoan GPI anchors were discussed based on what has been reported on literature. Results: There are many evidences that GPI anchors are crucial for parasite's survival and interaction with hosts' cells. Despite all GPI anchors contain a conserved glycan core, they present variations regarding structural features and biosynthetic pathways between organisms, which could offer adequate selectivity to validate GPI anchors as drug targets. Discussion was developed with focus on the following parasites: Trypanosoma brucei, Trypanosoma cruzi, Leishmania, Plasmodium falciparum and Toxoplasma gondii, causative agents of tropical neglected diseases. Conclusion: This review debates the main variances between parasitic and mammalian GPI anchor biosynthesis and structures, as well as clues for strategic development for new anti-parasitic therapies based on GPI anchors.

  Immunotherapy, protozoan, drug discovery, Glycosylphosphatidylinositol (GPI), lipopeptidophosphoglycans (LPPGs)

  NCBI PubMed ID: 28748758
  Publication DOI: 10.2174/0929867324666170727110801
  Journal NLM ID: 9440157
  Publisher: Saif Zone, Sharjah, U.A.E.: Bentham Science Publishers
  Correspondence: carronal@usp.br
  Institutions: School of Pharmaceutical Sciences of Ribeirão Preto - University of São Paulo, São Paulo, Brazil
  
   
  
  Trypanosoma brucei
  CSDB ID 7339 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 1860 [(M-292)+Na]2+
Trivial name: GPI of VSG (variant surface glycoprotein)
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_140425,IEDB_140426,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_145015,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,SB_191,SB_195,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 5977
  Nett IRE, Mehlert A, Lamont D, Ferguson MAJ "Application of electrospray mass spectrometry to the structural determination of glycosylphosphatidylinositol membrane anchors" - Glycobiology 20(5) (2010) 576-585
  

  The addition of glycosylphosphatidylinositol (GPI) anchors to proteins is an important posttranslational modification in eukaryotic cells. The complete structural elucidation of GPI anchors is a complex process that requires relatively large amounts of starting material. In this paper, we assess the degree of structural information that can be obtained by applying electrospray mass spectrometry and tandem mass spectrometry to permethylated GPI glycans prepared from a well-characterized GPI-anchored glycoprotein, the variant surface glycoprotein from Trypanosoma brucei. All GPI glycans contain a non-N-acetylated glucosamine residue, and permethylation leads to the formation of a fixed positive charge on the glycans, in the form of a quaternary amine. The permethylated glycans were detected as [M+Na]2+ ions, and tandem mass spectrometry of these ions produced substantial, albeit incomplete, structural information on the branching patterns and linkage types for various GPI glycoforms of the variant surface glycoprotein.

  mass spectrometry, Glycosylphosphatidylinositol, Trypanosoma brucei, variant surface glycoprotein, GPI anchor

  NCBI PubMed ID: 20100693
  Publication DOI: 10.1093/glycob/cwq007
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: m.a.j.ferguson@dundee.ac
  Institutions: Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK
  Methods: methylation, GC-MS, ESI-MS, ESI-MS/MS, HF treatment, permethylation
  
   
  
  Trypanosoma brucei 427 variant 121
  CSDB ID 7347 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: variant surface glycoproteins (VSG) GPI anchor
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 6015
  Tsai YH, Liu XY, Seeberger PH "Chemical Biology of Glycosylphosphatidylinositol Anchors" - Angewandte Chemie, International Edition 51(46) (2012) 11438-11456
  

  Glycosylphosphatidylinositols (GPIs) are complex glycolipids that are covalently linked to the C-terminus of proteins as a posttranslational modification. They anchor the attached protein to the cell membrane and are essential for normal functioning of eukaryotic cells. GPI-anchored proteins are structurally and functionally diverse. Many GPIs have been structurally characterized but comprehension of their biological functions, beyond the simple physical anchoring, remains largely speculative. Work on functional elucidation at a molecular level is still limited. This Review focuses on the roles of GPI unraveled by using synthetic molecules and summarizes the structural diversity of GPIs, as well as their biological and chemical syntheses.

  Oligosaccharides, vaccines, proteins, glycosylphosphatidylinositols, protein modifications

  Publication DOI: 10.1002/anie.201203912
  Journal NLM ID: 0370543
  Publisher: Weinheim: Wiley-VCH
  Correspondence: seeberger@mpikg.mpg.de
  Institutions: Department of Biomolecular Systems Max Planck Institute of Colloids and Interfaces Am M?hlenberg 1, 14424 Potsdam (Germany), Institute of Chemistry and Biochemistry Free University of Berlin Arnimallee 22, 14195 Berlin (Germany), Department of Chemistry, University of Pittsburgh 219 Parkman Avenue, Pittsburgh, PA 15260, USA
  
   
  
  Trypanosoma brucei 117
  CSDB ID 7385 (all data & tools)
• Article ID: 6016
  Tsai YH, Grube M, Seeberger PH, Silva DV "Glycosylphosphatidylinositols of Protozoan Parasites" - Trends in Glycoscience and Glycotechnology 24(140) (2012) 231-243
  

  Glycosylphosphatidylinositol (GPI) anchors are commonly found in all eukaryotic cells. However, compared to mammalian cells, protozoan parasites express about one hundred times more GPI glycolipids per cell. GPIs are commonly employed by the parasites to anchor surface antigens on the extracellular membrane, although not protein-linked or free GPIs can also be found. Parasitic GPIs are believed to regulate the immune response of the host by protozoa. However, a detailed structure function relationship of GPIs has not been established due to the difficulties in obtaining sufficient quantities of homogeneous material. This review summarizes the structures of characterized parasitic GPIs and their roles in triggering host immune responses. We focus on the recent progress in the chemical synthesis of GPI anchors and application of synthetic materials for development of vaccines and glycan arrays.

  glycosylation, vaccine, diagnostic, Glycosylphosphatidylinositol, trypanosomiasis

  Publication DOI: 10.4052/tigg.24.231
  Journal NLM ID: 9425898
  Correspondence: daniel.varon@mpikg.mpg.de
  Institutions: Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany
  
   
  
  Trypanosoma brucei 117
  CSDB ID 9490 (all data & tools)