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1. Compound ID: 347
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3HOMyr-(1-3)-+
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?%Ara-(1--P--1)--+ |
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Lau-(1-3)-3HOMyr-(1-3)-+ | |
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C16={11}-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN
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?%Arap4N-(1--P--4)--+ 3HOMyr-(1-2)-+ |
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Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_136907,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_534864,IEDB_581506
The structure is contained in the following publication(s):
- Article ID: 98
Therisod H, Karibian D, Perry MB, Caroff M "Structural analysis of Yersinia pseudotuberculosis ATCC 29833 lipid A" -
International Journal of Mass Spectrometry 219(3) (2002) 549-557
The Yersinia genus includes human and animal pathogens (plague, enterocolitis) as well as non-pathogens. The lipopolysaccharide of the facultative pathogen Yersinia pseudotuberculosis has been implicated in the invasiveness of these bacteria. In this work, we have investigated the fine structure of the lipid A isolated from Y. pseudotuberculosis lipopolysaccharide using chemical analyses, gas chromatography/mass spectrometry, plasma desorption mass spectrometry, and matrix-assisted laser desorption mass spectrometry. Arabinose (Ara) and aminoarabinose (Ara-4N) esterified the phosphates as in Yersinia pestis lipid A. The acylation of Y. pseudotuberculosis lipid A differed from those found in Yersinia enterocolitica, Yersinia ruckeri, and Y. pestis lipopolysaccharides (LPSs): in the distribution of fatty acids between the two glucosamines in the fully acylated hexaacyl molecular species and by the acyloxyacyl substitution at position C-2′, where the Y. pseudotuberculosis lipid A has a C14OC16 making it closest to that of Y. pestis.
lipid A, endotoxin, Yersinia pseudotuberculosis, Y. pseudotuberculosis, PDMS, MALDI
Publication DOI: 10.1016/S1387-3806(02)00706-6Journal NLM ID: 101137096Publisher: Elsevier
Correspondence: martine.caroff@bbmpc.u-psud.fr
Institutions: Equipe “Endotoxines”, UMR 8619 du CNRS, I.B.B.M.C., Université de Paris-Sud, F-Orsay, France, Institute for Biological Sciences, NRC, Ottawa, Ont., Canada
Methods: GC-MS, SDS-PAGE, TLC, ESI-MS, GC, MALDI-TOF MS, composition analysis, mild alkaline degradation, PD-MS
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2. Compound ID: 4392
Structure type: oligomer
Contained glycoepitopes: IEDB_581506
The structure is contained in the following publication(s):
- Article ID: 1656
Tropis M, Lemassu A, Vincent V, Daffé M "Structural elucidation of the predominant motifs of the major cell wall arabinogalactan antigens from the borderline species Tsukamurella paurometabolum and Mycobacterium fallax" -
Glycobiology 15(7) (2005) 677-686
Tsukamurella paurometabolum and Mycobacterium fallax are members of the suprageneric actinomycete group Corynebacterineae that possesses a cell wall skeleton composed of a peptidoglycan to which an arabinogalactan is covalently attached. This polysaccharide is further modified by esterification with C60-C80 mycolic acid residues in mycobacteria and T. paurometabolum. However, M. fallax and T. paurometabolum produce polyenoic (up to six double bonds) mycolic acids whereas the most common type of mycobacterial mycolates, called alpha-mycolates, are mono- and di-enoic or -cyclopropanated mycolic acids. To determine whether this difference also applied to the structures of cell wall arabinogalactans, competitive inhibition experiments using antibodies raised against the cell wall from Mycobacterium bovis and the arabinogalactans from T. paurometabolum and M. fallax were performed. They demonstrated the structural identity between the polysaccharide of M. fallax and those of mycobacteria and showed a strong similarity between the latter polysaccharides and that of T. paurometabolum. Structural analyses of the per-O-alkylated alditol fragments derived from the polysaccharides by gas chromatography-mass spectrometry (GC-MS) and 13C nuclear magnetic resonance (NMR) spectroscopy of the intact solubilized polysaccharides demonstrated that the polysaccharides from the two species analyzed contained all the major structural features previously characterized in mycobacterial arabinogalactans. These include (1) the homogalactan of alterning 5-linked galactofuranosyl (Galf) and 6-linked Galf residues, (2) a linear 5-linked arabino furanosyl (Araf), (3) a β-Araf-(1→2)-α-Araf disaccharide branched on both position 3 and position 5 of an α-Araf unit, and (4) a 5-linked-α-Araf unit branched on both position 3 and position 5 of an α-Araf residue. The polysaccharide from T. paurometabolum possesses additional structural domains composed of a terminal (t) Araf directly linked to either a 5-linked-α-Araf or to both position 3 and position 5 of a 3,5-linked α-Araf unit. Both the remarkable similarity of arabinogalactans from Corynebacterineae and their genus- and/or species-specificities are reflected in their 13C NMR spectra that may be used as a valuable help in the identification of members of the actinomycete group
cell wall, Mycobacterium, arabinogalactan, Tsukamurella
NCBI PubMed ID: 15761023Publication DOI: 10.1093/glycob/cwi052Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Departement Mecanismes Moleculaires des Infections Mycobacteriennes, Institut de Pharmacologie et Biologie Structurale, UMR 5089 du Centre National de la Recherche Scientifique et de l'Universite Paul Sabatier, 31077 Toulouse cedex 04, France
Methods: NMR
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3. Compound ID: 5724
Structure type: oligomer
Compound class: lipophosphoglycan, LPG
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2500
Ng K, Handman E, Bacic A "Biosynthesis of lipophosphoglycan from Leishmania major: characterization of (β1-3)-galactosyltransferase(s)" -
Glycobiology 4(6) (1994) 845-853
Lipophosphoglycan (LPG) is the major cell surface molecule of promastigotes of all Leishmania species. It is comprised of three domains: a conserved GPI anchor linked to a repeating phosphorylated disaccharide (P2; PO4-6-Gal(β 1-4)Man(α 1-) backbone variously substituted with galactose, glucose and arabinose residues in L.major and capped with a neutral oligosaccharide. Using a microsomal membrane preparation from L.major, we have been able to demonstrate that galactose from UDP-[14C]galactose can be transferred to an endogenous acceptor, characterized as LPG. An in vitro assay was established, based on anion-exchange HPLC, that concurrently identifies and quantitates the products of the galactosyltransferases. We show that the products formed are [14C]galactose-labelled P3 (PO4-6-[Gal(β 1-3)]Gal(β 1-4)Man(α 1-), P4b (PO4-6-[Gal(β 1-3)Gal(β 1-3)]Gal(β 1-4)Man(α 1-) and P5b(PO4-6-[Gal(β 1-3)Gal(β 1-3)Gal(β 1-3)]Gal(β 1- 4)Man(α 1-). These are major galactosylated repeating units of the backbone of L.major LPG. The same products are also formed when LPG from L.donovani, which contains an unbranched backbone of P2 repeats, is used as an exogenous acceptor with L.major microsomal membranes and UDP-[14C]galactose. In addition, no formation of radioactive backbone repeats (P2) was detected in membrane incubations containing UDP-[14C]galactose with or without added unlabelled GDP-mannose, indicating that the addition of the (β 1-3)-linked galactose branches is independent of the synthesis of the repeating disaccharide (P2) backbone. Preliminary kinetic analyses suggest that the addition of multiple (β 1-3)-linked galactose residues may be catalysed by more than one (β 1-3) galactosyltransferase. The (β 1-3)galactosyltransferase(s) activity was not detected in microsomal membrane preparations from promastigotes of L.donovani.
biosynthesis, glycosyltransferases, Galactosyltransferases, leishmania, lipophosphoglycan
NCBI PubMed ID: 7734847Publication DOI: 10.1093/glycob/4.6.845Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria, Australia
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4. Compound ID: 5726
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P-6)-+
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b-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-D-Man |
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Structure type: oligomer
Compound class: lipophosphoglycan, LPG
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2500
Ng K, Handman E, Bacic A "Biosynthesis of lipophosphoglycan from Leishmania major: characterization of (β1-3)-galactosyltransferase(s)" -
Glycobiology 4(6) (1994) 845-853
Lipophosphoglycan (LPG) is the major cell surface molecule of promastigotes of all Leishmania species. It is comprised of three domains: a conserved GPI anchor linked to a repeating phosphorylated disaccharide (P2; PO4-6-Gal(β 1-4)Man(α 1-) backbone variously substituted with galactose, glucose and arabinose residues in L.major and capped with a neutral oligosaccharide. Using a microsomal membrane preparation from L.major, we have been able to demonstrate that galactose from UDP-[14C]galactose can be transferred to an endogenous acceptor, characterized as LPG. An in vitro assay was established, based on anion-exchange HPLC, that concurrently identifies and quantitates the products of the galactosyltransferases. We show that the products formed are [14C]galactose-labelled P3 (PO4-6-[Gal(β 1-3)]Gal(β 1-4)Man(α 1-), P4b (PO4-6-[Gal(β 1-3)Gal(β 1-3)]Gal(β 1-4)Man(α 1-) and P5b(PO4-6-[Gal(β 1-3)Gal(β 1-3)Gal(β 1-3)]Gal(β 1- 4)Man(α 1-). These are major galactosylated repeating units of the backbone of L.major LPG. The same products are also formed when LPG from L.donovani, which contains an unbranched backbone of P2 repeats, is used as an exogenous acceptor with L.major microsomal membranes and UDP-[14C]galactose. In addition, no formation of radioactive backbone repeats (P2) was detected in membrane incubations containing UDP-[14C]galactose with or without added unlabelled GDP-mannose, indicating that the addition of the (β 1-3)-linked galactose branches is independent of the synthesis of the repeating disaccharide (P2) backbone. Preliminary kinetic analyses suggest that the addition of multiple (β 1-3)-linked galactose residues may be catalysed by more than one (β 1-3) galactosyltransferase. The (β 1-3)galactosyltransferase(s) activity was not detected in microsomal membrane preparations from promastigotes of L.donovani.
biosynthesis, glycosyltransferases, Galactosyltransferases, leishmania, lipophosphoglycan
NCBI PubMed ID: 7734847Publication DOI: 10.1093/glycob/4.6.845Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria, Australia
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5. Compound ID: 5953
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P-6)-+
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a-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp |
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Structure type: oligomer
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2652
McConville MJ, Thomas-Oates JE, Ferguson MAJ, Homans SW "Structure of the lipophosphoglycan from Leishmania major" -
Journal of Biological Chemistry 265 (1990) 19611-19623
The major cell surface glycoconjugate of the parasitic protozoan Leishmania major is a heterogeneous lipophosphoglycan. It has a tripartite structure, consisting of a phosphoglycan (Mr 5,000-40,000), a variably phosphorylated hexasaccharide glycan core, and a lysoalkylphosphatidylinositol (lysoalkyl-PI) lipid anchor. The structures of the phosphoglycan and the hexasaccharide core were determined by monosaccharide analysis, methylation analysis, fast atom bombardment-mass spectrometry, one- and two-dimensional 500-MHz (correlated spectroscopy (COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA] 1H NMR spectroscopy, and exoglycosidase digestions. The phosphoglycan consists of eight types of phosphorylated oligosaccharide repeats which have the general structure, [formula: see text] where R = H, Galp(β1-3), Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3), Glcp(β1-3)Galp(β1-3), Galp(β1-3)Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3)Galp(β1-3), or Arap(α1-2)Galp(β1-3)Galp(β1-3)Galp(β1-3)Galp(β1-3), and where all the monosaccharides, including arabinose, are in the D-configuration. The average number of repeat units/molecule (n) is 27. Data are presented which suggest that the nonreducing terminus of the phosphoglycan is capped exclusively with the neutral disaccharide Manp(α1-2)Manp α1-. The structure of the glycan core was determined to be, [formula: see text] where approximately 60% of the mannose residues distal to the glucosamine are phosphorylated and where the inositol is part of the lysoalkyl-PI lipid moiety containing predominantly 24:0 and 26:0 alkyl chains. The unusual galactofuranose residue is in the β-configuration, correcting a previous report where this residue was identified as α-Galf. Although most of the phosphorylated repeat units are attached to the terminal galactose 6-phosphate of the core to form a linear lipophosphoglycan (LPG) molecule, some of the mannose 6-phosphate residues may also be substituted to form a Y-shaped molecule. The L. major LPG is more complex than the previously characterized LPG from Leishmania donovani, although both LPGs have the same repeating backbone structure and glycolipid anchor. Finally we show that the LPG anchor is structurally related to the major glycolipid species of L. major, indicating that some of these glycolipids may have a function as precursors to LPG.
NCBI PubMed ID: 2246247Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry, The University, Dundee, United Kingdom
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6. Compound ID: 5954
Structure type: oligomer
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2652
McConville MJ, Thomas-Oates JE, Ferguson MAJ, Homans SW "Structure of the lipophosphoglycan from Leishmania major" -
Journal of Biological Chemistry 265 (1990) 19611-19623
The major cell surface glycoconjugate of the parasitic protozoan Leishmania major is a heterogeneous lipophosphoglycan. It has a tripartite structure, consisting of a phosphoglycan (Mr 5,000-40,000), a variably phosphorylated hexasaccharide glycan core, and a lysoalkylphosphatidylinositol (lysoalkyl-PI) lipid anchor. The structures of the phosphoglycan and the hexasaccharide core were determined by monosaccharide analysis, methylation analysis, fast atom bombardment-mass spectrometry, one- and two-dimensional 500-MHz (correlated spectroscopy (COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA] 1H NMR spectroscopy, and exoglycosidase digestions. The phosphoglycan consists of eight types of phosphorylated oligosaccharide repeats which have the general structure, [formula: see text] where R = H, Galp(β1-3), Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3), Glcp(β1-3)Galp(β1-3), Galp(β1-3)Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3)Galp(β1-3), or Arap(α1-2)Galp(β1-3)Galp(β1-3)Galp(β1-3)Galp(β1-3), and where all the monosaccharides, including arabinose, are in the D-configuration. The average number of repeat units/molecule (n) is 27. Data are presented which suggest that the nonreducing terminus of the phosphoglycan is capped exclusively with the neutral disaccharide Manp(α1-2)Manp α1-. The structure of the glycan core was determined to be, [formula: see text] where approximately 60% of the mannose residues distal to the glucosamine are phosphorylated and where the inositol is part of the lysoalkyl-PI lipid moiety containing predominantly 24:0 and 26:0 alkyl chains. The unusual galactofuranose residue is in the β-configuration, correcting a previous report where this residue was identified as α-Galf. Although most of the phosphorylated repeat units are attached to the terminal galactose 6-phosphate of the core to form a linear lipophosphoglycan (LPG) molecule, some of the mannose 6-phosphate residues may also be substituted to form a Y-shaped molecule. The L. major LPG is more complex than the previously characterized LPG from Leishmania donovani, although both LPGs have the same repeating backbone structure and glycolipid anchor. Finally we show that the LPG anchor is structurally related to the major glycolipid species of L. major, indicating that some of these glycolipids may have a function as precursors to LPG.
NCBI PubMed ID: 2246247Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry, The University, Dundee, United Kingdom
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7. Compound ID: 5957
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P-6)-+
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a-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp |
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Structure type: oligomer
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2652
McConville MJ, Thomas-Oates JE, Ferguson MAJ, Homans SW "Structure of the lipophosphoglycan from Leishmania major" -
Journal of Biological Chemistry 265 (1990) 19611-19623
The major cell surface glycoconjugate of the parasitic protozoan Leishmania major is a heterogeneous lipophosphoglycan. It has a tripartite structure, consisting of a phosphoglycan (Mr 5,000-40,000), a variably phosphorylated hexasaccharide glycan core, and a lysoalkylphosphatidylinositol (lysoalkyl-PI) lipid anchor. The structures of the phosphoglycan and the hexasaccharide core were determined by monosaccharide analysis, methylation analysis, fast atom bombardment-mass spectrometry, one- and two-dimensional 500-MHz (correlated spectroscopy (COSY), homonuclear Hartmann-Hahn spectroscopy (HOHAHA] 1H NMR spectroscopy, and exoglycosidase digestions. The phosphoglycan consists of eight types of phosphorylated oligosaccharide repeats which have the general structure, [formula: see text] where R = H, Galp(β1-3), Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3), Glcp(β1-3)Galp(β1-3), Galp(β1-3)Galp(β1-3)Galp(β1-3), Arap(α1-2)Galp(β1-3)Galp(β1-3), or Arap(α1-2)Galp(β1-3)Galp(β1-3)Galp(β1-3)Galp(β1-3), and where all the monosaccharides, including arabinose, are in the D-configuration. The average number of repeat units/molecule (n) is 27. Data are presented which suggest that the nonreducing terminus of the phosphoglycan is capped exclusively with the neutral disaccharide Manp(α1-2)Manp α1-. The structure of the glycan core was determined to be, [formula: see text] where approximately 60% of the mannose residues distal to the glucosamine are phosphorylated and where the inositol is part of the lysoalkyl-PI lipid moiety containing predominantly 24:0 and 26:0 alkyl chains. The unusual galactofuranose residue is in the β-configuration, correcting a previous report where this residue was identified as α-Galf. Although most of the phosphorylated repeat units are attached to the terminal galactose 6-phosphate of the core to form a linear lipophosphoglycan (LPG) molecule, some of the mannose 6-phosphate residues may also be substituted to form a Y-shaped molecule. The L. major LPG is more complex than the previously characterized LPG from Leishmania donovani, although both LPGs have the same repeating backbone structure and glycolipid anchor. Finally we show that the LPG anchor is structurally related to the major glycolipid species of L. major, indicating that some of these glycolipids may have a function as precursors to LPG.
NCBI PubMed ID: 2246247Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry, The University, Dundee, United Kingdom
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8. Compound ID: 6170
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P-6)-+
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b-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp-(1--/P-backbone repeat/ |
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Structure type: oligomer
Aglycon: P-backbone repeat
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2759
Kelleher M, Curtis JM, Sacks DL, Handman E, Bacic A "Epitope mapping of monoclonal antibodies directed against lipophosphoglycan of Leishmania major promastigotes" -
Molecular and Biochemical Parasitology 66 (1994) 187-200
Monoclonal antibodies (MAbs) were generated against Leishmania major promastigote lipophosphoglycan (LPG) to use as tools in defining functional epitopes of this major cell surface glycoconjugate. Epitope mapping of four MAbs, designated 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2, revealed that the phosphorylated oligosaccharide repeat unit PO4-6[Gal(β1-3)]Gal(β1-4)Man α1-, P3, is a highly immunogenic epitope which has previously been demonstrated, by chemical analyses, to be a repeat unit specific to L. major. Two antibodies, 4A2-A2 and 5E10-F2, also recognised the repeat unit PO4-6[Ara(β1-2)Gal(β1-3)]Gal(β1-4)Man α1-, 4Pa, with less affinity than P3, while 2G11-A3 recognised P4a with greater affinity than for P3. The L. major metacyclic-specific antibody 3F12 only recognised repeat units terminating with arabinose residues. In particular, 3F12 recognised P4a, which is upregulated in metacyclic LPG compared to the procyclic form of the molecule. The oligosaccharides P3, P4a and P5a are specific to L. major LPG. The epitopes of 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2 were found on the cell surface and in the flagellar pocket of both procyclic and metacyclic V121 promastigotes, but were only detected at very low levels on amastigotes. The repeat unit P3 is able to inhibit attachment of procyclic promastigotes to the midgut of the sandfly vector, but neither Fab fragments of the four antibodies nor purified P3 could inhibit attachment of metacyclic promastigotes to the macrophage cell line J774. It was also shown that human sera from patients with cutaneous leishmaniasis recognised purified P3. The data suggests that while P3 is an immunogen in the natural course of infection of the human host, P3 plays no role in attachment and internalisation of promastigotes into the macrophages of the mammalian host.
NCBI PubMed ID: 7808469Journal NLM ID: 8006324Institutions: Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Melbourne, Victoria, Australia
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9. Compound ID: 6171
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P-6)-+
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b-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp-(1--/P-backbone repeat/ |
Show graphically |
Structure type: oligomer
Aglycon: P-backbone repeat
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2759
Kelleher M, Curtis JM, Sacks DL, Handman E, Bacic A "Epitope mapping of monoclonal antibodies directed against lipophosphoglycan of Leishmania major promastigotes" -
Molecular and Biochemical Parasitology 66 (1994) 187-200
Monoclonal antibodies (MAbs) were generated against Leishmania major promastigote lipophosphoglycan (LPG) to use as tools in defining functional epitopes of this major cell surface glycoconjugate. Epitope mapping of four MAbs, designated 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2, revealed that the phosphorylated oligosaccharide repeat unit PO4-6[Gal(β1-3)]Gal(β1-4)Man α1-, P3, is a highly immunogenic epitope which has previously been demonstrated, by chemical analyses, to be a repeat unit specific to L. major. Two antibodies, 4A2-A2 and 5E10-F2, also recognised the repeat unit PO4-6[Ara(β1-2)Gal(β1-3)]Gal(β1-4)Man α1-, 4Pa, with less affinity than P3, while 2G11-A3 recognised P4a with greater affinity than for P3. The L. major metacyclic-specific antibody 3F12 only recognised repeat units terminating with arabinose residues. In particular, 3F12 recognised P4a, which is upregulated in metacyclic LPG compared to the procyclic form of the molecule. The oligosaccharides P3, P4a and P5a are specific to L. major LPG. The epitopes of 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2 were found on the cell surface and in the flagellar pocket of both procyclic and metacyclic V121 promastigotes, but were only detected at very low levels on amastigotes. The repeat unit P3 is able to inhibit attachment of procyclic promastigotes to the midgut of the sandfly vector, but neither Fab fragments of the four antibodies nor purified P3 could inhibit attachment of metacyclic promastigotes to the macrophage cell line J774. It was also shown that human sera from patients with cutaneous leishmaniasis recognised purified P3. The data suggests that while P3 is an immunogen in the natural course of infection of the human host, P3 plays no role in attachment and internalisation of promastigotes into the macrophages of the mammalian host.
NCBI PubMed ID: 7808469Journal NLM ID: 8006324Institutions: Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Melbourne, Victoria, Australia
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10. Compound ID: 6173
|
P-6)-+
|
b-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp-(1--/P-backbone repeat/ |
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Structure type: oligomer
Aglycon: P-backbone repeat
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2759
Kelleher M, Curtis JM, Sacks DL, Handman E, Bacic A "Epitope mapping of monoclonal antibodies directed against lipophosphoglycan of Leishmania major promastigotes" -
Molecular and Biochemical Parasitology 66 (1994) 187-200
Monoclonal antibodies (MAbs) were generated against Leishmania major promastigote lipophosphoglycan (LPG) to use as tools in defining functional epitopes of this major cell surface glycoconjugate. Epitope mapping of four MAbs, designated 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2, revealed that the phosphorylated oligosaccharide repeat unit PO4-6[Gal(β1-3)]Gal(β1-4)Man α1-, P3, is a highly immunogenic epitope which has previously been demonstrated, by chemical analyses, to be a repeat unit specific to L. major. Two antibodies, 4A2-A2 and 5E10-F2, also recognised the repeat unit PO4-6[Ara(β1-2)Gal(β1-3)]Gal(β1-4)Man α1-, 4Pa, with less affinity than P3, while 2G11-A3 recognised P4a with greater affinity than for P3. The L. major metacyclic-specific antibody 3F12 only recognised repeat units terminating with arabinose residues. In particular, 3F12 recognised P4a, which is upregulated in metacyclic LPG compared to the procyclic form of the molecule. The oligosaccharides P3, P4a and P5a are specific to L. major LPG. The epitopes of 4A2-A2, 2G11-A3, 5E6-D10 and 5E10-F2 were found on the cell surface and in the flagellar pocket of both procyclic and metacyclic V121 promastigotes, but were only detected at very low levels on amastigotes. The repeat unit P3 is able to inhibit attachment of procyclic promastigotes to the midgut of the sandfly vector, but neither Fab fragments of the four antibodies nor purified P3 could inhibit attachment of metacyclic promastigotes to the macrophage cell line J774. It was also shown that human sera from patients with cutaneous leishmaniasis recognised purified P3. The data suggests that while P3 is an immunogen in the natural course of infection of the human host, P3 plays no role in attachment and internalisation of promastigotes into the macrophages of the mammalian host.
NCBI PubMed ID: 7808469Journal NLM ID: 8006324Institutions: Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Melbourne, Victoria, Australia
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11. Compound ID: 6383
|
b-D-Galp-(1-4)-+
|
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1--P--6)--+ a-D-Glcp-(1--P--6)--+
| |
/Variants 0/-{{{-b-D-Galp-(1-4)-a-D-Manp-(1--P--6)--}}}/n=14-36/-a-D-Galp-(1-6)-a-D-Galp-(1-3)-b-D-Galf-(1-3)-a-D-Manp-(1-3)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(1--P--3)--Gro1ALK
/Variants 0/ is:
{{{-b-D-Gal-(1-3)-}}}/n=4-10/-b-D-Gal-(1-3)-
OR (exclusively)
b-Arap-(1-2)-{{{-b-D-Gal-(1-3)-}}}/n=0-2/-b-D-Gal-(1-3)- |
Show graphically |
Structure type: oligomer
Trivial name: GPI-anchor
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_134624,IEDB_136044,IEDB_136095,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141794,IEDB_141807,IEDB_141830,IEDB_142349,IEDB_142350,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_144996,IEDB_144998,IEDB_145002,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_156494,IEDB_164174,IEDB_189518,IEDB_190606,IEDB_433717,IEDB_474450,IEDB_581506,IEDB_983930,IEDB_983931,SB_136,SB_163,SB_165,SB_166,SB_187,SB_192,SB_195,SB_196,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- 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: 8373346Publication DOI: 10.1042/bj2940305Journal NLM ID: 2984726RPublisher: 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
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12. Compound ID: 6386
|
/Variants 0/-+
|
-6)-b-D-Galp-(1-4)-a-D-Manp-(1-P-
/Variants 0/ is:
{{{-b-D-Gal-(1-3)-}}}/n=1-11/-b-D-Gal-(1-3)-
OR (exclusively)
b-Arap-(1-2)-{{{-b-D-Gal-(1-3)-}}}/n=0-2/-b-D-Gal-(1-3)- |
Show graphically |
Structure type: polymer biological repeating unit
; n=14,30
Aglycon: ->6)core of GPI-anchor
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136095,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_144996,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- 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: 8373346Publication DOI: 10.1042/bj2940305Journal NLM ID: 2984726RPublisher: 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
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13. Compound ID: 6389
|
Mycolic-(?-5)-+
|
Mycolic-(?-5)-b-D-Araf-(1-2)-b-D-Araf-(1-5)-+
|
Mycolic-(?-5)-+ |
| |
Mycolic-(?-5)-b-D-Araf-(1-2)-b-D-Araf-(1-3)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-+
|
Mycolic-(?-5)-+ |
| |
Mycolic-(?-5)-b-D-Araf-(1-2)-b-D-Araf-(1-5)-+ |
| |
Mycolic-(?-5)-+ | |
| | |
Mycolic-(?-5)-b-D-Araf-(1-2)-b-D-Araf-(1-3)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-3)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-b-D-Araf-(1-5)-D-Ara |
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Structure type: oligomer
Contained glycoepitopes: IEDB_159255,IEDB_581506
The structure is contained in the following publication(s):
- Article ID: 1776
Besra GS, Khoo KH, McNeil MR, Dell A, Morris HR, Brennan PJ "A new interpretation of the structure of the mycolyl-arabinogalactan complex of Mycobacterium tuberculosis as revealed through characterization of oligoglycosylalditol fragments by fast-atom bombardment mass spectrometry and 1H nuclear magnetic resonance spectroscopy" -
Biochemistry 34 (1995) 4257-4266
Previous structural analysis of small oligosaccharide fragments had allowed the recognition of several small structural motifs within arabinogalactan, the dominant cell was structural polysaccharide of Mycobacterium tuberculosis. To determine how these motifs are connected to one another to form the complete polymer, oligosaccharide fragments containing up to 26 glycosyl residues were released by gentle acid hydrolysis of the per-O-methylated arabinogalactan, converted to fully per-O-alkylated oligoglycosylalditols, and purified by high-performance liquid chromatography, and the molecular weights and alkylation patterns of the resultant oligoglycosyl fragments were determined by fast atom bombardment mass spectrometry. The results, combined with previous studies, allowed further understanding of the intricate structural features of the nonreducing ends of arabinogalactan. Thus, the extended nonreducing ends of the arabinan were shown to consist of a tricosaarabinoside (23-mer). We reason that three such arabinan motifs are attached to the homogalactan component or arabinogalactan, which was previously shown to consist of alternating 5- and 6-linked β-D-galactofuranosyl residues. Using the same approach as applied to the arabinan branches, an extended stretch of the galactan was isolated that consisted of at least 23 alternating β-1,6 and β-1,5 D-Galf residues, devoid of any branching, demonstrating that the points of attachment of the arabinan chains to galactan are close to the reducing end of galactan, which itself is linked to peptidoglycan via the linker disaccharide phosphate L-Rhap-(1→3)-α-D-GlcNAc-P. By nuclear magnetic resonance analysis, the L-Rhap was shown to be in the alpha configuration. The long-chain α-alkyl-β-hydroxy mycolic acids, known to occupy the 5-positions of both the terminal β-D-Araf and internal 2-α-D-Araf residues of the terminal branched pentaarabinosyl motif, are now shown to be nonacylated at the beta-hydroxy function. Lack of acylation points to intramolecular hydrogen bonding between the beta-hydroxyl and carbonyl functions of the mycolic acid, providing a highly ordered arrangement of mycolic acids in accord with evolving models of the orientation of the cell wall polymers in mycobacterial cell walls. A revised model is proposed for the composition and orientation of the mycolyl-arabinogalactan in the cell walls of M. tuberculosis, which should increase our understanding of cell wall hydrophobicity, impermeability, and role in disease pathogenesis.
NCBI PubMed ID: 7703239Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Department of Microbiology, Colorado State University, Fort Collins 80523, USA
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14. Compound ID: 6404
|
?%a-D-Arap-(1-2)-+
|
/Variants 0/-?%b-D-Galp-(1-3)-+
|
---P--6)-b-D-Galp-(1-4)-a-D-Manp-(1-
/Variants 0/ is:
?%b-D-Glcp-(1-3)-
OR (exclusively)
?%b-D-Galp-(1-3)-+
|
?%a-D-Arap-(1-2)-?%b-D-Galp-(1-3)- |
Show graphically |
Structure type: polymer biological repeating unit
; n=~27
Aglycon: core
Trivial name: GPI-anchor
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_144996,IEDB_146664,IEDB_152206,IEDB_156494,IEDB_190606,IEDB_433717,IEDB_581506,IEDB_983930,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2881
Ilg T, Harbecke D, Wiese M, Overath P "Monoclonal antibodies directed against Leishmania secreted acidphosphatase and lipophosphoglycan. Partial characterization of privateand public epitopes" -
European Journal of Biochemistry 217 (1993) 603-615
Leishmania promastigotes, the stage of the parasite characteristic for the sandfly vector, express an abundant glycoconjugate, called lipophosphoglycan, at their surface. Lipophosphoglycan consists of lysoalkyl-sn-glycerophosphoinositol linked to a phosphosaccharide core conserved in all species, which is connected to PO4-6Gal β1,4Man α1 repeats with species-specific substitutions at the Gal residue; the repeats are capped by conserved and species-specific oligosaccharides. Most Leishmania species also secrete an acid phosphatase, which, in Leishmania mexicana, is a filamentous complex composed of a phosphorylated glycoprotein and non-covalently associated proteo-(high-molecular-mass)phosphoglycan. The secreted acid phosphatase complex was used as an antigen to derive a panel of monoclonal antibodies (mAbs). A total of 25 mAbs (17 novel and 8 previously described) were tested by different techniques for their specificity against lipophosphoglycan and secreted acid phosphatase from several Leishmania species. This comparison and the modification of the antigens by chemical or enzymic treatments allowed a classification of the mAbs into several groups. First, from 25 mAbs examined, 22 recognize lipophosphoglycan and the enzyme complex of L. mexicana; only three are specific for secreted acid phosphatase. Two of the latter group are also directed against carbohydrate structures, whereas the third mAb recognizes the 100-kDa polypeptide of the complex. The secreted acid-phosphatase-specific class detects antigen in the flagellar pocket of promastigotes while all anti-lipophosphoglycan mAbs bind to the cell surface. Second, all 15 anti-lipophosphoglycan mAbs investigated in detail appear to be directed against the phosphosaccharide repeats or the cap structure rather than the phosphosaccharide core. Two mAbs recognize terminal cap-structures containing Man α1,2Man residues. Four antibodies are specific for L. mexicana and are probably directed against PO4-6[Glc β1,3]Gal β1,4Man α1 repeats while six mAbs react with the unmodified repeats. Two antibodies specific for Leishmania major recognize Gal β1,3-substituted repeats unique for lipophosphoglycan from this species. Analysis by immunoblotting indicates that the high-molecular-mass proteo-phosphoglycan of L. mexicana secreted acid phosphatase carries epitopes for all anti-lipophosphoglycan mAbs suggesting the presence of capped phosphosaccharide repeats while the enzymically active glycoprotein subunit is modified by caps but probably not by repeats. In the case of Leishmania donovani secreted acid phosphatase, the enzymically active polypeptide may be directly modified by repeats. The mAbs are used to characterize changes in lipophosphoglycan structure, which occur in culture during the transition of promastigotes from the logarithmic to the stationary growth phase. Furthermore, testing the mAbs against seven species demonstrates their potential for serotyping Leishmania.
NCBI PubMed ID: 7693464Publication DOI: 10.1111/j.1432-1033.1993.tb18283.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Max-Planck-Institut für Biologie, Tübingen, Germany
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15. Compound ID: 6405
|
?%a-D-Arap-(1-2)-+
|
/Variants 1/-?%b-D-Galp-(1-3)-+ a-D-Glcp-(1--P--6)--+
| |
/Variants 2/-a-D-Manp-(1--P--6)--{{{-b-D-Galp-(1-4)-a-D-Manp-(1--P--6)--}}}/n=27/-a-D-Galp-(1-6)-a-D-Galp-(1-3)-b-D-Galf-(1-3)-a-D-Manp-(1-3)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-INO-(1--P--3)--Gro-(1-1)-ALK
/Variants 0/ is:
?%a-D-Arap-(1-2)-?%b-D-Galp-(1-3)-
OR (exclusively)
a-D-Arap-(1-2)-
/Variants 1/ is:
?%b-D-Glcp-(1-3)-
OR (exclusively)
?%b-D-Galp-(1-3)-+
|
?%a-D-Arap-(1-2)-?%b-D-Galp-(1-3)-
/Variants 2/ is:
/Variants 0/-?%b-D-Galp-(1-4)-
OR (exclusively)
?%a-D-Manp-(1-2)- |
Show graphically |
Structure type: oligomer
Trivial name: GPI-anchor
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_134624,IEDB_136044,IEDB_136095,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144996,IEDB_144998,IEDB_145002,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_156494,IEDB_164174,IEDB_190606,IEDB_433717,IEDB_474450,IEDB_581506,IEDB_983930,IEDB_983931,SB_136,SB_163,SB_165,SB_166,SB_187,SB_192,SB_195,SB_196,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2881
Ilg T, Harbecke D, Wiese M, Overath P "Monoclonal antibodies directed against Leishmania secreted acidphosphatase and lipophosphoglycan. Partial characterization of privateand public epitopes" -
European Journal of Biochemistry 217 (1993) 603-615
Leishmania promastigotes, the stage of the parasite characteristic for the sandfly vector, express an abundant glycoconjugate, called lipophosphoglycan, at their surface. Lipophosphoglycan consists of lysoalkyl-sn-glycerophosphoinositol linked to a phosphosaccharide core conserved in all species, which is connected to PO4-6Gal β1,4Man α1 repeats with species-specific substitutions at the Gal residue; the repeats are capped by conserved and species-specific oligosaccharides. Most Leishmania species also secrete an acid phosphatase, which, in Leishmania mexicana, is a filamentous complex composed of a phosphorylated glycoprotein and non-covalently associated proteo-(high-molecular-mass)phosphoglycan. The secreted acid phosphatase complex was used as an antigen to derive a panel of monoclonal antibodies (mAbs). A total of 25 mAbs (17 novel and 8 previously described) were tested by different techniques for their specificity against lipophosphoglycan and secreted acid phosphatase from several Leishmania species. This comparison and the modification of the antigens by chemical or enzymic treatments allowed a classification of the mAbs into several groups. First, from 25 mAbs examined, 22 recognize lipophosphoglycan and the enzyme complex of L. mexicana; only three are specific for secreted acid phosphatase. Two of the latter group are also directed against carbohydrate structures, whereas the third mAb recognizes the 100-kDa polypeptide of the complex. The secreted acid-phosphatase-specific class detects antigen in the flagellar pocket of promastigotes while all anti-lipophosphoglycan mAbs bind to the cell surface. Second, all 15 anti-lipophosphoglycan mAbs investigated in detail appear to be directed against the phosphosaccharide repeats or the cap structure rather than the phosphosaccharide core. Two mAbs recognize terminal cap-structures containing Man α1,2Man residues. Four antibodies are specific for L. mexicana and are probably directed against PO4-6[Glc β1,3]Gal β1,4Man α1 repeats while six mAbs react with the unmodified repeats. Two antibodies specific for Leishmania major recognize Gal β1,3-substituted repeats unique for lipophosphoglycan from this species. Analysis by immunoblotting indicates that the high-molecular-mass proteo-phosphoglycan of L. mexicana secreted acid phosphatase carries epitopes for all anti-lipophosphoglycan mAbs suggesting the presence of capped phosphosaccharide repeats while the enzymically active glycoprotein subunit is modified by caps but probably not by repeats. In the case of Leishmania donovani secreted acid phosphatase, the enzymically active polypeptide may be directly modified by repeats. The mAbs are used to characterize changes in lipophosphoglycan structure, which occur in culture during the transition of promastigotes from the logarithmic to the stationary growth phase. Furthermore, testing the mAbs against seven species demonstrates their potential for serotyping Leishmania.
NCBI PubMed ID: 7693464Publication DOI: 10.1111/j.1432-1033.1993.tb18283.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Max-Planck-Institut für Biologie, Tübingen, Germany
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Next 15 structure(s)
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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