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1. Compound ID: 2021
R-Lac-(2-4)-b-D-Glcp-(1-4)-a-L-Rhap-(1-4)-a-D-GlcpA-(1-3)-+
|
-3)-b-D-Galp-(1-4)-a-D-Manp-(1-3)-a-D-Galp-(1- |
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Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_115013,IEDB_115136,IEDB_130645,IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_149558,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_433717,IEDB_885823,IEDB_918314,IEDB_983930,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_44,SB_67,SB_7,SB_72,SB_87,SB_88
The structure is contained in the following publication(s):
- Article ID: 619
Aucken HM, Wilkinson SG, Pitt TL "Re-evaluation of the serotypes of Serratia marcescens and separation into two schemes based on lipopolysaccharide (O) and capsular polysaccharide (K) antigens" -
Microbiology 144 (1998) 639-653
Chemical and serological analysis has revealed that many of the 29 O serotype reference strains of Serratia marcescens contain both neutral and acidic polysaccharides which correspond to LPS O antigens and capsular K antigens, respectively. New O and K antigen typing schemes have therefore been devised, based on the known chemical structures of the surface polysaccharides of the organism. These schemes were designed to allow the specific detection of these antigens on unknown strains using ELISAs. O antigens were detected using whole cells cultured in broth then autoclaved to remove capsular material, while K antigens were detected using formolized whole cells which had been cultured on glycerol agar to enhance capsule production. After testing with the 29 reference strains as well as 423 distinct clinical strains, it was apparent that different aspects of chemical structure were associated with different degrees of serological reactivity and the typing schemes were modified further to accommodate this. In general, the O antigen repeating unit structures were chemically simple with di- or trisaccharide backbones. Serological specificity was often provided solely by the presence or absence of an O-acetyl substituent, or a change in the linkage between two sugar residues. Five of the O serotypes in the new scheme were represented by 12 of the 29 reference strains, while three reference strains lacked O antigens altogether, resulting in the elimination of 10 of the original O types. In contrast, the K antigen repeating unit structures were more complex and chemically diverse, having at least four sugar residues. Three K types were each seen in two reference strains while 12 of the 29 reference strains were acapsular. Thus, the resulting schemes contain 19 O types and 14 K types and allow the definitive serotype identification of S. marcescens.
Lipopolysaccharide, antigen, LPS, structure, K-antigen, O-antigen, capsular polysaccharide, Serratia marcescens, Serratia, serotyping, O-serotype
NCBI PubMed ID: 9534235Journal NLM ID: 0376646Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
Correspondence: haucken@phls.co.uk
Institutions: Laboratory of Hospital Infection, Central Public Health Laboratory, 61 Colindale Avenue, London NW9 5HT, UK, School of Chemistry, The University, Hull HU6 7RX, UK
Methods: NMR, SDS-PAGE, ELISA, chromatography, Quellung reaction, serum adsorption assays
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2. Compound ID: 2362
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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3. Compound ID: 2383
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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4. Compound ID: 2384
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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5. Compound ID: 2385
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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6. Compound ID: 2386
Structure type: oligomer
; 583.5
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_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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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7. Compound ID: 2387
Structure type: oligomer
; 745.6
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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8. Compound ID: 2388
P-6)-+
|
b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-b-D-Galp-(1-4)-D-Man |
Show graphically |
Structure type: oligomer
; 907.6
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_158555,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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9. Compound ID: 2389
Structure type: oligomer
; 583.5
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_190606,IEDB_241118,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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10. Compound ID: 2390
Structure type: oligomer
; 745.6
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_241118,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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11. Compound ID: 2391
Structure type: oligomer
; 745.6
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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12. Compound ID: 2392
P-6)-+
|
P-6)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-b-D-Galp-(1-4)-D-Man |
Show graphically |
Structure type: oligomer
; 825.5
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_241118,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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13. Compound ID: 2393
P-6)-+
|
P-6)-b-D-Galp-(1-3)-b-D-Glcp-(1-3)-b-D-Galp-(1-4)-D-Man |
Show graphically |
Structure type: oligomer
; 825.5
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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14. Compound ID: 2394
P-6)-+
|
P-6)-b-D-Galp-(1-3)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-b-D-Galp-(1-4)-D-Man |
Show graphically |
Structure type: oligomer
; 987.8
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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15. Compound ID: 2395
P-6)-+ P-6)-+
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P-6)-b-D-Glcp-(1-3)-b-D-Glcp-(1-3)-b-D-Galp-(1-4)-D-Man |
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Structure type: oligomer
; 905.8
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_136100,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153543,IEDB_190606,IEDB_241118,IEDB_433717,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: 824
Ilg T, Craik D, Currie G, Multhaup G, Bacic A "Stage-specific proteophosphoglycan from Leishmania mexicana antastigotes - Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides" -
Journal of Biological Chemistry 273(22) (1998) 13509-13523
Intracellular amastigotes of the protozoan parasite Leishmania mexicana secrete a macromolecular proteo-phosphoglycan (aPPG) into the phagolysosome of their host cell, the mammalian macrophage. The structures of aPPG glycans were analyzed by a combination of high pH anion exchange high pressure liquid chromatography, gas chromatography-mass spectrometry, enzymatic digestions, electrospray-mass spectrometry as well as 1H and 31P NMR spectroscopy. Some glycans are identical to oligosaccharides known from Leishmania mexicana promastigote lipophosphoglycan and secreted acid phosphatase. However, the majority of the aPPG glycans represent amastigote stage-specific and novel structures. These include neutral glycans ( [Glc(bl-3)(n=1-2)]Gal(bl-4)Man, Gal(bl-3)Gal(bl-4)Man, Gal(bl-3)Glc(bl-3)Gal(bl-4)Man ), several monophosphorylated glycans containing the conserved phosphodisaccharide backbone (R-3-[PO4-6-Gal] (bl-4)Man) but carrying stage-specific modifications ( R = Gal(bl-,[Glc(bl-3)(n=1-2)Glc(bl- ), and monophosphorylated aPPG tri- and tetrasaccharides that are uniquely phosphorylated on the terminal hexose ( PO4-6-Glc(bl-3)Gal(bl-4)Man, PO4-6-Glc(bl-3)Glc(bl-3)Gal(bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Gal(b1-4)Man ). In addition aPPG contains highly unusual di- and triphosphorylated glycans whose major species are PO4-6-Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(b1-3)[PO4-6-Gal](bl-4)Man, PO4-6-Gal(bl-3)Glc(bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)[PO4-6-Gal](b1-4)Man, PO4-6-Gal(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man, and PO4-6-Glc(bl-3)[PO4-6-Glc](bl-3)Glc(bl-3)[PO4-6-Gal](bl-4)Man. These glycans are linked together by the conserved phosphodiester R-Man-(a1-PO4-6)-Gal-R or the novel phosphodiester R-Man-(a1-PO4-6)-Glc-R and are connected to Ser(P) of the protein backbone most likely via the linkage R-Man-(a1-PO4-Ser). The variety of stage-specific glycan structures in Leishmania mexicana aPPG suggests the presence of developmentally regulated amastigote glycosyl-transferases which may be potential anti-parasite drug targets.
oligosaccharide, structural, characterization, Oligosaccharides, leishmania
NCBI PubMed ID: 9593686Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: thomas.ilg@tuebingen.mpg.de
Institutions: Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Victoria 3052, Australia, Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia, the Centre for Drug Design and Development, University of Queensland, Brisbane, Queensland 4072, Australia, Centre for Molecular Biology, Heidelberg, Germany
Methods: NMR-2D, GC-MS, ESI-MS, enzymatic digestion, HPAE-HPLC
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