Found 15 structures.
Displayed structures from 1 to 15
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1. Compound ID: 5731
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P-6)-+
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b-D-Galp-(1-3)-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_136103,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_156494,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: 2501
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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2. Compound ID: 5958
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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: 2653
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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3. Compound ID: 5963
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P-6)-+
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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_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: 2653
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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4. Compound ID: 6175
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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: 2760
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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5. Compound ID: 6388
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b-D-Galp-(1-4)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1--P--6)--+ a-D-Glcp-(1--P--6)--+
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/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)-L-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)- |
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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_142488,IEDB_143632,IEDB_144983,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: 1736
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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6. Compound ID: 6390
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{{{-b-D-Galp-(1-3)-}}}/n=1-11/-b-D-Gal-(1-3)-+
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-6)-b-D-Galp-(1-4)-a-D-Manp-(1-P- |
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Structure type: polymer biological repeating unit
; n=36
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_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: 1736
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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7. Compound ID: 6391
|
/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)- |
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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: 1736
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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8. Compound ID: 6409
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?%a-D-Arap-(1-2)-+
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/Variants 0/-?%b-D-Galp-(1-3)-+
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---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)- |
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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: 2882
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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9. Compound ID: 6410
|
?%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: 2882
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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10. Compound ID: 6414
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?%b-D-Galp-(1-4)-+
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?%a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1--P--6)--+ a-D-Glcp-(1--P--6)--+
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?%b-D-Arap-(1-2)-{{{-b-D-Galp-(1-3)-}}}/n=0-2/-85%b-D-Galp-(1-3)-{{{-b-D-Galp-(1-4)-a-D-Manp-(1--P--6)--}}}/n=30/-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 |
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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_142488,IEDB_143632,IEDB_144983,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: 2501
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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11. Compound ID: 6425
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a-D-Manp-(1-2)-a-D-Manp-(1--P--6)--+ P-6)-+ /Variants 0/-+
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?%a-D-Arap-(1-2)-{{{-b-D-Galp-(1-3)-}}}/n=0-2/-b-D-Galp-(1-3)-{{{-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)-L-myoIno-(1--P--3)--Gro
/Variants 0/ is:
Lig-(1-1)-
OR (exclusively)
Crt-(1-1)- |
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Structure type: oligomer
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_143632,IEDB_144983,IEDB_144996,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_156494,IEDB_164174,IEDB_190606,IEDB_433717,IEDB_474450,IEDB_581506,IEDB_983930,SB_136,SB_163,SB_165,SB_166,SB_187,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: 2653
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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12. Compound ID: 6428
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a-D-Arap-(1-2)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-+
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---P--6)-b-D-Galp-(1-4)-a-D-Manp-(1- |
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Structure type: polymer biological repeating unit
Aglycon: core
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_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: 2659
McConville MJ, Homans SW "Identification of the defect in lipophosphoglycan biosynthesis in a non-pathogenic strain of Leishmania major" -
Journal of Biological Chemistry 267 (1992) 5855-5861
The major macromolecule on the surface of the protozoan parasite, Leishmania major, is a complex lipophosphoglycan (LPG), which is anchored to the plasma membrane by an inositol-containing phospholipid. A defect in LPG biosynthesis is thought to be responsible for the avirulence of the L. major strain LRC L119 in mice. In order to identify the nature of this defect we have characterized two truncated forms of LPG, which are accumulated in this strain, by one- and two-dimensional 500-MHz 1H NMR spectroscopy, two-dimensional heteronuclear 1H-31P NMR spectroscopy, methylation analysis, and exoglycosidase digestions. The structures of these glycoinositolphospholipids, termed GIPL-4 and -6, are as follows: [formula: see text] The glycan moieties of GIPL-4 and -6 are identical to the anchor region of LPG, which is also substituted with a Glc-1-PO4 residue in approximately 60% of the structures. However, instead of being capped with chains of phosphorylated oligosaccharide repeat units, both glycan moieties terminate in Man α1-PO4, suggesting that the defect in LPG biosynthesis is in the transfer of galactose to this residue to form the disaccharide backbone of the first repeat unit. These results indicate that the phosphoglycan moiety of LPG is essential for intracellular survival of the parasite and have implications for LPG biosynthesis.
NCBI PubMed ID: 1532574Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry, University of Dundee, United Kingdom
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13. Compound ID: 6429
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P-6)-+ 60%a-D-Glcp-(1--P--6)--+
| |
?%a-D-Arap-(1-2)-{{{-b-D-Galp-(1-3)-}}}/n=0-2/-b-D-Galp-(1-3)-{{{-b-D-Galp-(1-4)-a-D-Manp-(1--P--6)--}}}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)-L-myoIno-(1--P--3)--Gro-(1-1)-ALK |
Show graphically |
Structure type: oligomer
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_134624,IEDB_136044,IEDB_136095,IEDB_136100,IEDB_136101,IEDB_136103,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,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_163,SB_165,SB_166,SB_187,SB_192,SB_195,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 2659
McConville MJ, Homans SW "Identification of the defect in lipophosphoglycan biosynthesis in a non-pathogenic strain of Leishmania major" -
Journal of Biological Chemistry 267 (1992) 5855-5861
The major macromolecule on the surface of the protozoan parasite, Leishmania major, is a complex lipophosphoglycan (LPG), which is anchored to the plasma membrane by an inositol-containing phospholipid. A defect in LPG biosynthesis is thought to be responsible for the avirulence of the L. major strain LRC L119 in mice. In order to identify the nature of this defect we have characterized two truncated forms of LPG, which are accumulated in this strain, by one- and two-dimensional 500-MHz 1H NMR spectroscopy, two-dimensional heteronuclear 1H-31P NMR spectroscopy, methylation analysis, and exoglycosidase digestions. The structures of these glycoinositolphospholipids, termed GIPL-4 and -6, are as follows: [formula: see text] The glycan moieties of GIPL-4 and -6 are identical to the anchor region of LPG, which is also substituted with a Glc-1-PO4 residue in approximately 60% of the structures. However, instead of being capped with chains of phosphorylated oligosaccharide repeat units, both glycan moieties terminate in Man α1-PO4, suggesting that the defect in LPG biosynthesis is in the transfer of galactose to this residue to form the disaccharide backbone of the first repeat unit. These results indicate that the phosphoglycan moiety of LPG is essential for intracellular survival of the parasite and have implications for LPG biosynthesis.
NCBI PubMed ID: 1532574Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Biochemistry, University of Dundee, United Kingdom
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14. Compound ID: 6446
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P-6)-+
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b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-b-D-Galp-(1-4)-a-D-Manp-(1--/backbone repeat/ |
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Structure type: oligomer
Aglycon: 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_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: 2760
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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15. Compound ID: 6617
|
8%b-D-Galp-(1-3)-48%b-D-Galp-(1-3)-b-D-Galp-(1-3)-+
|
---P--6)-b-D-Galp-(1-4)-a-D-Manp-(1- |
Show graphically |
Structure type: polymer biological repeating unit
Aglycon: C6 of phosphatidylinositol
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_144983,IEDB_144996,IEDB_152206,IEDB_156494,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: 2882
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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Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (permanent record IDs):
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