Show legend Show as text

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

• 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: 2246247
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Department of Biochemistry, The University, Dundee, United Kingdom
  
   
  
  Leishmania major
  CSDB ID 135965 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: type-2 GIPL, type-2 GIPL, iM2
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_534865,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 5889
  Assis RR, Ibraim IC, Noronha FS, Turco SJ, Soares RP "Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure" - PLoS Neglected Tropical Diseases 6(2) (2012) e1543
  

  The essential role of the lipophosphoglycan (LPG) of Leishmania in innate immune response has been extensively reported. However, information about the role of the LPG-related glycoinositolphospholipids (GIPLs) is limited, especially with respect to the New World species of Leishmania. GIPLs are low molecular weight molecules covering the parasite surface and are similar to LPG in sharing a common lipid backbone and a glycan motif containing up to 7 sugars. Critical aspects of their structure and functions are still obscure in the interaction with the vertebrate host. In this study, we evaluated the role of those molecules in two medically important South American species Leishmania infantum and L. braziliensis, causative agents of visceral (VL) and cutaneous Leishmaniasis (CL), respectively. GIPLs derived from both species did not induce NO or TNF-α production by non-primed murine macrophages. Additionally, primed macrophages from mice (BALB/c, C57BL/6, TLR2-/- and TLR4-/-) exposed to GIPLs from both species, with exception to TNF-α, did not produce any of the cytokines analyzed (IL1-β, IL-2, IL-4, IL-5, IL-10, IL-12p40, IFN-γ) or p38 activation. GIPLs induced the production of TNF-α and NO by C57BL/6 mice, primarily via TLR4. Pre incubation of macrophages with GIPLs reduced significantly the amount of NO and IL-12 in the presence of IFN-γ or lipopolysaccharide (LPS), which was more pronounced with L. braziliensis GIPLs. This inhibition was reversed after PI-specific phospholipase C treatment. A structural analysis of the GIPLs showed that L. infantum has manose rich GIPLs, suggestive of type I and Hybrid GIPLs while L. braziliensis has galactose rich GIPLs, suggestive of Type II GIPLs. In conclusion, there are major differences in the structure and composition of GIPLs from L. braziliensis and L. infantum. Also, GIPLs are important inhibitory molecules during the interaction with macrophages.

  carbohydrate, interaction, leishmania, lipophosphoglycan, Leishmania infantum

  NCBI PubMed ID: 22389743
  Publication DOI: 10.1371/journal.pntd.0001543
  Journal NLM ID: 101291488
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: rsoares@cpqrr.fiocruz.br
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz - FIOCRUZ, Belo Horizonte, Brazil, Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, United States of America
  Methods: gel filtration, SDS-PAGE, TLC, ELISA, acid hydrolysis, deamination, FACE, HPLC, immunoblotting, statistical analysis, flow cytometry analysis, cytokine production
  
   
  
  Leishmania donovani, Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5460 (all data & tools)
• Article ID: 5890
  Assis RR, Ibraim IC, Nogueira PM, Soares RP, Turco SJ "Glycoconjugates in New World species of Leishmania: Polymorphisms in lipophosphoglycan and glycoinositolphospholipids and interaction with hosts" - Biochimica et Biophysica Acta: General Subjects 1820(9) (2012) 1354-1365
  

  Background: Protozoan parasites of the genus Leishmania cause a number of important diseases in humans and undergo a complex life cycle, alternating between a sand fly vector and vertebrate hosts. The parasites have a remarkable capacity to avoid destruction in which surface molecules are determinant for survival. Amongst the many surface molecules of Leishmania, the glycoconjugates are known to play a central role in host-parasite interactions and are the focus of this review. Scope of the review: The most abundant and best studied glycoconjugates are the Lipophosphoglycans (LPGs) and glycoinositolphospholipids (GIPLs). This review summarizes the main studies on structure and biological functions of these molecules in New World Leishmania species. Major conclusions: LPG and GIPLs are complex molecules that display inter- and intraspecies polymorphisms. They are key elements for survival inside the vector and to modulate the vertebrate immune response during infection. General significance: Most of the studies on glycoconjugates focused on Old World Leishmania species. Here, it is reported some of the studies involving New World species and their biological significance on host-parasite interaction. This article is part of a Special Issue entitled Glycoproteomics.

  leishmania, lipophosphoglycan, glycoinositolphospholipids, Host–parasite interaction, New World

  NCBI PubMed ID: 22093608
  Publication DOI: 10.1016/j.bbagen.2011.11.001
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: S.J. Turco
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz, FIOCRUZ, Av. Augusto de Lima, 1715, Belo Horizonte, MG 30190-002, Brazil, Department of Biochemistry, University of Kentucky Medical Center, 741 South Limestone, Lexington, KY 40536, USA
  
   
  
  Leishmania donovani, Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5467 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: type-2 GIPL-1, type-2 GIPL, GIPL-1
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_534865,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 5889
  Assis RR, Ibraim IC, Noronha FS, Turco SJ, Soares RP "Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure" - PLoS Neglected Tropical Diseases 6(2) (2012) e1543
  

  The essential role of the lipophosphoglycan (LPG) of Leishmania in innate immune response has been extensively reported. However, information about the role of the LPG-related glycoinositolphospholipids (GIPLs) is limited, especially with respect to the New World species of Leishmania. GIPLs are low molecular weight molecules covering the parasite surface and are similar to LPG in sharing a common lipid backbone and a glycan motif containing up to 7 sugars. Critical aspects of their structure and functions are still obscure in the interaction with the vertebrate host. In this study, we evaluated the role of those molecules in two medically important South American species Leishmania infantum and L. braziliensis, causative agents of visceral (VL) and cutaneous Leishmaniasis (CL), respectively. GIPLs derived from both species did not induce NO or TNF-α production by non-primed murine macrophages. Additionally, primed macrophages from mice (BALB/c, C57BL/6, TLR2-/- and TLR4-/-) exposed to GIPLs from both species, with exception to TNF-α, did not produce any of the cytokines analyzed (IL1-β, IL-2, IL-4, IL-5, IL-10, IL-12p40, IFN-γ) or p38 activation. GIPLs induced the production of TNF-α and NO by C57BL/6 mice, primarily via TLR4. Pre incubation of macrophages with GIPLs reduced significantly the amount of NO and IL-12 in the presence of IFN-γ or lipopolysaccharide (LPS), which was more pronounced with L. braziliensis GIPLs. This inhibition was reversed after PI-specific phospholipase C treatment. A structural analysis of the GIPLs showed that L. infantum has manose rich GIPLs, suggestive of type I and Hybrid GIPLs while L. braziliensis has galactose rich GIPLs, suggestive of Type II GIPLs. In conclusion, there are major differences in the structure and composition of GIPLs from L. braziliensis and L. infantum. Also, GIPLs are important inhibitory molecules during the interaction with macrophages.

  carbohydrate, interaction, leishmania, lipophosphoglycan, Leishmania infantum

  NCBI PubMed ID: 22389743
  Publication DOI: 10.1371/journal.pntd.0001543
  Journal NLM ID: 101291488
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: rsoares@cpqrr.fiocruz.br
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz - FIOCRUZ, Belo Horizonte, Brazil, Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, United States of America
  Methods: gel filtration, SDS-PAGE, TLC, ELISA, acid hydrolysis, deamination, FACE, HPLC, immunoblotting, statistical analysis, flow cytometry analysis, cytokine production
  
   
  
  Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5461 (all data & tools)
• Article ID: 5890
  Assis RR, Ibraim IC, Nogueira PM, Soares RP, Turco SJ "Glycoconjugates in New World species of Leishmania: Polymorphisms in lipophosphoglycan and glycoinositolphospholipids and interaction with hosts" - Biochimica et Biophysica Acta: General Subjects 1820(9) (2012) 1354-1365
  

  Background: Protozoan parasites of the genus Leishmania cause a number of important diseases in humans and undergo a complex life cycle, alternating between a sand fly vector and vertebrate hosts. The parasites have a remarkable capacity to avoid destruction in which surface molecules are determinant for survival. Amongst the many surface molecules of Leishmania, the glycoconjugates are known to play a central role in host-parasite interactions and are the focus of this review. Scope of the review: The most abundant and best studied glycoconjugates are the Lipophosphoglycans (LPGs) and glycoinositolphospholipids (GIPLs). This review summarizes the main studies on structure and biological functions of these molecules in New World Leishmania species. Major conclusions: LPG and GIPLs are complex molecules that display inter- and intraspecies polymorphisms. They are key elements for survival inside the vector and to modulate the vertebrate immune response during infection. General significance: Most of the studies on glycoconjugates focused on Old World Leishmania species. Here, it is reported some of the studies involving New World species and their biological significance on host-parasite interaction. This article is part of a Special Issue entitled Glycoproteomics.

  leishmania, lipophosphoglycan, glycoinositolphospholipids, Host–parasite interaction, New World

  NCBI PubMed ID: 22093608
  Publication DOI: 10.1016/j.bbagen.2011.11.001
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: S.J. Turco
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz, FIOCRUZ, Av. Augusto de Lima, 1715, Belo Horizonte, MG 30190-002, Brazil, Department of Biochemistry, University of Kentucky Medical Center, 741 South Limestone, Lexington, KY 40536, USA
  
   
  
  Leishmania major
  CSDB ID 6190 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: type-2 GIPL-2, type-2 GIPL, GIPL-2
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_534865,IEDB_983930,SB_197,SB_44,SB_67,SB_7,SB_72

• Article ID: 5889
  Assis RR, Ibraim IC, Noronha FS, Turco SJ, Soares RP "Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure" - PLoS Neglected Tropical Diseases 6(2) (2012) e1543
  

  The essential role of the lipophosphoglycan (LPG) of Leishmania in innate immune response has been extensively reported. However, information about the role of the LPG-related glycoinositolphospholipids (GIPLs) is limited, especially with respect to the New World species of Leishmania. GIPLs are low molecular weight molecules covering the parasite surface and are similar to LPG in sharing a common lipid backbone and a glycan motif containing up to 7 sugars. Critical aspects of their structure and functions are still obscure in the interaction with the vertebrate host. In this study, we evaluated the role of those molecules in two medically important South American species Leishmania infantum and L. braziliensis, causative agents of visceral (VL) and cutaneous Leishmaniasis (CL), respectively. GIPLs derived from both species did not induce NO or TNF-α production by non-primed murine macrophages. Additionally, primed macrophages from mice (BALB/c, C57BL/6, TLR2-/- and TLR4-/-) exposed to GIPLs from both species, with exception to TNF-α, did not produce any of the cytokines analyzed (IL1-β, IL-2, IL-4, IL-5, IL-10, IL-12p40, IFN-γ) or p38 activation. GIPLs induced the production of TNF-α and NO by C57BL/6 mice, primarily via TLR4. Pre incubation of macrophages with GIPLs reduced significantly the amount of NO and IL-12 in the presence of IFN-γ or lipopolysaccharide (LPS), which was more pronounced with L. braziliensis GIPLs. This inhibition was reversed after PI-specific phospholipase C treatment. A structural analysis of the GIPLs showed that L. infantum has manose rich GIPLs, suggestive of type I and Hybrid GIPLs while L. braziliensis has galactose rich GIPLs, suggestive of Type II GIPLs. In conclusion, there are major differences in the structure and composition of GIPLs from L. braziliensis and L. infantum. Also, GIPLs are important inhibitory molecules during the interaction with macrophages.

  carbohydrate, interaction, leishmania, lipophosphoglycan, Leishmania infantum

  NCBI PubMed ID: 22389743
  Publication DOI: 10.1371/journal.pntd.0001543
  Journal NLM ID: 101291488
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: rsoares@cpqrr.fiocruz.br
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz - FIOCRUZ, Belo Horizonte, Brazil, Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, United States of America
  Methods: gel filtration, SDS-PAGE, TLC, ELISA, acid hydrolysis, deamination, FACE, HPLC, immunoblotting, statistical analysis, flow cytometry analysis, cytokine production
  
   
  
  Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5462 (all data & tools)
• Article ID: 5890
  Assis RR, Ibraim IC, Nogueira PM, Soares RP, Turco SJ "Glycoconjugates in New World species of Leishmania: Polymorphisms in lipophosphoglycan and glycoinositolphospholipids and interaction with hosts" - Biochimica et Biophysica Acta: General Subjects 1820(9) (2012) 1354-1365
  

  Background: Protozoan parasites of the genus Leishmania cause a number of important diseases in humans and undergo a complex life cycle, alternating between a sand fly vector and vertebrate hosts. The parasites have a remarkable capacity to avoid destruction in which surface molecules are determinant for survival. Amongst the many surface molecules of Leishmania, the glycoconjugates are known to play a central role in host-parasite interactions and are the focus of this review. Scope of the review: The most abundant and best studied glycoconjugates are the Lipophosphoglycans (LPGs) and glycoinositolphospholipids (GIPLs). This review summarizes the main studies on structure and biological functions of these molecules in New World Leishmania species. Major conclusions: LPG and GIPLs are complex molecules that display inter- and intraspecies polymorphisms. They are key elements for survival inside the vector and to modulate the vertebrate immune response during infection. General significance: Most of the studies on glycoconjugates focused on Old World Leishmania species. Here, it is reported some of the studies involving New World species and their biological significance on host-parasite interaction. This article is part of a Special Issue entitled Glycoproteomics.

  leishmania, lipophosphoglycan, glycoinositolphospholipids, Host–parasite interaction, New World

  NCBI PubMed ID: 22093608
  Publication DOI: 10.1016/j.bbagen.2011.11.001
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: S.J. Turco
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz, FIOCRUZ, Av. Augusto de Lima, 1715, Belo Horizonte, MG 30190-002, Brazil, Department of Biochemistry, University of Kentucky Medical Center, 741 South Limestone, Lexington, KY 40536, USA
  
   
  
  Leishmania major, Leishmania mexicana
  CSDB ID 5468 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: type-2 GIPL-3, type-2 GIPL, GIPL-3
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_134624,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_534865,IEDB_983930,SB_163,SB_197,SB_44,SB_67,SB_7,SB_72

• Article ID: 5889
  Assis RR, Ibraim IC, Noronha FS, Turco SJ, Soares RP "Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure" - PLoS Neglected Tropical Diseases 6(2) (2012) e1543
  

  The essential role of the lipophosphoglycan (LPG) of Leishmania in innate immune response has been extensively reported. However, information about the role of the LPG-related glycoinositolphospholipids (GIPLs) is limited, especially with respect to the New World species of Leishmania. GIPLs are low molecular weight molecules covering the parasite surface and are similar to LPG in sharing a common lipid backbone and a glycan motif containing up to 7 sugars. Critical aspects of their structure and functions are still obscure in the interaction with the vertebrate host. In this study, we evaluated the role of those molecules in two medically important South American species Leishmania infantum and L. braziliensis, causative agents of visceral (VL) and cutaneous Leishmaniasis (CL), respectively. GIPLs derived from both species did not induce NO or TNF-α production by non-primed murine macrophages. Additionally, primed macrophages from mice (BALB/c, C57BL/6, TLR2-/- and TLR4-/-) exposed to GIPLs from both species, with exception to TNF-α, did not produce any of the cytokines analyzed (IL1-β, IL-2, IL-4, IL-5, IL-10, IL-12p40, IFN-γ) or p38 activation. GIPLs induced the production of TNF-α and NO by C57BL/6 mice, primarily via TLR4. Pre incubation of macrophages with GIPLs reduced significantly the amount of NO and IL-12 in the presence of IFN-γ or lipopolysaccharide (LPS), which was more pronounced with L. braziliensis GIPLs. This inhibition was reversed after PI-specific phospholipase C treatment. A structural analysis of the GIPLs showed that L. infantum has manose rich GIPLs, suggestive of type I and Hybrid GIPLs while L. braziliensis has galactose rich GIPLs, suggestive of Type II GIPLs. In conclusion, there are major differences in the structure and composition of GIPLs from L. braziliensis and L. infantum. Also, GIPLs are important inhibitory molecules during the interaction with macrophages.

  carbohydrate, interaction, leishmania, lipophosphoglycan, Leishmania infantum

  NCBI PubMed ID: 22389743
  Publication DOI: 10.1371/journal.pntd.0001543
  Journal NLM ID: 101291488
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: rsoares@cpqrr.fiocruz.br
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz - FIOCRUZ, Belo Horizonte, Brazil, Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, United States of America
  Methods: gel filtration, SDS-PAGE, TLC, ELISA, acid hydrolysis, deamination, FACE, HPLC, immunoblotting, statistical analysis, flow cytometry analysis, cytokine production
  
   
  
  Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5463 (all data & tools)
• Article ID: 5890
  Assis RR, Ibraim IC, Nogueira PM, Soares RP, Turco SJ "Glycoconjugates in New World species of Leishmania: Polymorphisms in lipophosphoglycan and glycoinositolphospholipids and interaction with hosts" - Biochimica et Biophysica Acta: General Subjects 1820(9) (2012) 1354-1365
  

  Background: Protozoan parasites of the genus Leishmania cause a number of important diseases in humans and undergo a complex life cycle, alternating between a sand fly vector and vertebrate hosts. The parasites have a remarkable capacity to avoid destruction in which surface molecules are determinant for survival. Amongst the many surface molecules of Leishmania, the glycoconjugates are known to play a central role in host-parasite interactions and are the focus of this review. Scope of the review: The most abundant and best studied glycoconjugates are the Lipophosphoglycans (LPGs) and glycoinositolphospholipids (GIPLs). This review summarizes the main studies on structure and biological functions of these molecules in New World Leishmania species. Major conclusions: LPG and GIPLs are complex molecules that display inter- and intraspecies polymorphisms. They are key elements for survival inside the vector and to modulate the vertebrate immune response during infection. General significance: Most of the studies on glycoconjugates focused on Old World Leishmania species. Here, it is reported some of the studies involving New World species and their biological significance on host-parasite interaction. This article is part of a Special Issue entitled Glycoproteomics.

  leishmania, lipophosphoglycan, glycoinositolphospholipids, Host–parasite interaction, New World

  NCBI PubMed ID: 22093608
  Publication DOI: 10.1016/j.bbagen.2011.11.001
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: S.J. Turco
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz, FIOCRUZ, Av. Augusto de Lima, 1715, Belo Horizonte, MG 30190-002, Brazil, Department of Biochemistry, University of Kentucky Medical Center, 741 South Limestone, Lexington, KY 40536, USA
  
   
  
  Leishmania major, Leishmania mexicana
  CSDB ID 5469 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: type-2 GIPL-A, type-2 GIPL, GIPL-A
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_534865,IEDB_983930,SB_197,SB_44,SB_67,SB_7,SB_72

• Article ID: 5889
  Assis RR, Ibraim IC, Noronha FS, Turco SJ, Soares RP "Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure" - PLoS Neglected Tropical Diseases 6(2) (2012) e1543
  

  The essential role of the lipophosphoglycan (LPG) of Leishmania in innate immune response has been extensively reported. However, information about the role of the LPG-related glycoinositolphospholipids (GIPLs) is limited, especially with respect to the New World species of Leishmania. GIPLs are low molecular weight molecules covering the parasite surface and are similar to LPG in sharing a common lipid backbone and a glycan motif containing up to 7 sugars. Critical aspects of their structure and functions are still obscure in the interaction with the vertebrate host. In this study, we evaluated the role of those molecules in two medically important South American species Leishmania infantum and L. braziliensis, causative agents of visceral (VL) and cutaneous Leishmaniasis (CL), respectively. GIPLs derived from both species did not induce NO or TNF-α production by non-primed murine macrophages. Additionally, primed macrophages from mice (BALB/c, C57BL/6, TLR2-/- and TLR4-/-) exposed to GIPLs from both species, with exception to TNF-α, did not produce any of the cytokines analyzed (IL1-β, IL-2, IL-4, IL-5, IL-10, IL-12p40, IFN-γ) or p38 activation. GIPLs induced the production of TNF-α and NO by C57BL/6 mice, primarily via TLR4. Pre incubation of macrophages with GIPLs reduced significantly the amount of NO and IL-12 in the presence of IFN-γ or lipopolysaccharide (LPS), which was more pronounced with L. braziliensis GIPLs. This inhibition was reversed after PI-specific phospholipase C treatment. A structural analysis of the GIPLs showed that L. infantum has manose rich GIPLs, suggestive of type I and Hybrid GIPLs while L. braziliensis has galactose rich GIPLs, suggestive of Type II GIPLs. In conclusion, there are major differences in the structure and composition of GIPLs from L. braziliensis and L. infantum. Also, GIPLs are important inhibitory molecules during the interaction with macrophages.

  carbohydrate, interaction, leishmania, lipophosphoglycan, Leishmania infantum

  NCBI PubMed ID: 22389743
  Publication DOI: 10.1371/journal.pntd.0001543
  Journal NLM ID: 101291488
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: rsoares@cpqrr.fiocruz.br
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz - FIOCRUZ, Belo Horizonte, Brazil, Department of Biochemistry, University of Kentucky Medical Center, Lexington, Kentucky, United States of America
  Methods: gel filtration, SDS-PAGE, TLC, ELISA, acid hydrolysis, deamination, FACE, HPLC, immunoblotting, statistical analysis, flow cytometry analysis, cytokine production
  
   
  
  Leishmania major, Leishmania mexicana, Leishmania panamensis
  CSDB ID 5464 (all data & tools)
• Article ID: 5890
  Assis RR, Ibraim IC, Nogueira PM, Soares RP, Turco SJ "Glycoconjugates in New World species of Leishmania: Polymorphisms in lipophosphoglycan and glycoinositolphospholipids and interaction with hosts" - Biochimica et Biophysica Acta: General Subjects 1820(9) (2012) 1354-1365
  

  Background: Protozoan parasites of the genus Leishmania cause a number of important diseases in humans and undergo a complex life cycle, alternating between a sand fly vector and vertebrate hosts. The parasites have a remarkable capacity to avoid destruction in which surface molecules are determinant for survival. Amongst the many surface molecules of Leishmania, the glycoconjugates are known to play a central role in host-parasite interactions and are the focus of this review. Scope of the review: The most abundant and best studied glycoconjugates are the Lipophosphoglycans (LPGs) and glycoinositolphospholipids (GIPLs). This review summarizes the main studies on structure and biological functions of these molecules in New World Leishmania species. Major conclusions: LPG and GIPLs are complex molecules that display inter- and intraspecies polymorphisms. They are key elements for survival inside the vector and to modulate the vertebrate immune response during infection. General significance: Most of the studies on glycoconjugates focused on Old World Leishmania species. Here, it is reported some of the studies involving New World species and their biological significance on host-parasite interaction. This article is part of a Special Issue entitled Glycoproteomics.

  leishmania, lipophosphoglycan, glycoinositolphospholipids, Host–parasite interaction, New World

  NCBI PubMed ID: 22093608
  Publication DOI: 10.1016/j.bbagen.2011.11.001
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: S.J. Turco
  Institutions: Centro de Pesquisas René Rachou, Fundação Oswaldo Cruz, FIOCRUZ, Av. Augusto de Lima, 1715, Belo Horizonte, MG 30190-002, Brazil, Department of Biochemistry, University of Kentucky Medical Center, 741 South Limestone, Lexington, KY 40536, USA
  
   
  
  Leishmania major
  CSDB ID 5470 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GIPL
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

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

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

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

  Publication DOI: 10.2174/1874421401004010084
  Journal NLM ID: 101552240
  Publisher: Hilversum: Bentham Science Publishers
  Correspondence: eliana.bergter@micro.ufrj.br
  Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes (IMPPG), Centro de Ciências da Saúde (CCS) Universidade Federal do Rio de Janeiro (UFRJ), Bloco I, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
  
   
  
  Trypanosoma cruzi Y
  CSDB ID 5482 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GIPL
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

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

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

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

  Publication DOI: 10.2174/1874421401004010084
  Journal NLM ID: 101552240
  Publisher: Hilversum: Bentham Science Publishers
  Correspondence: eliana.bergter@micro.ufrj.br
  Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes (IMPPG), Centro de Ciências da Saúde (CCS) Universidade Federal do Rio de Janeiro (UFRJ), Bloco I, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
  
   
  
  Trypanosoma cruzi
  CSDB ID 5483 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GIPL
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

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

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

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

  Publication DOI: 10.2174/1874421401004010084
  Journal NLM ID: 101552240
  Publisher: Hilversum: Bentham Science Publishers
  Correspondence: eliana.bergter@micro.ufrj.br
  Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes (IMPPG), Centro de Ciências da Saúde (CCS) Universidade Federal do Rio de Janeiro (UFRJ), Bloco I, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
  
   
  
  Trypanosoma cruzi Y
  CSDB ID 5484 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GIPL - Type 1
Compound class: glycoinositol phospholipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141181,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 5962
  Mattois EC, Tonelli RR, Colli W, Alves MJ "The Gp85 surface glycoproteins from Trypanosoma cruzi" - Subcellular Biochemistry 74 (2014) 151-180
  

  Trypanosoma cruzi strains show distinctive characteristics as genetic polymorphism and infectivity. Large repertoires of molecules, such as the Gp85 glycoproteins, members of the Gp85/Trans-sialidase superfamily, as well as multiple signaling pathways, are associated with invasion of mammalian cells by the parasite. Due to the large number of expressed members, encoded by more than 700 genes, the research focused on this superfamily conserved sequences is discussed. Binding sites to laminin have been identified at the N-terminus of the Gp85 molecules. Interestingly, the T. cruzi protein phosphorylation profile is changed upon parasite binding to laminin (or fibronectin), particularly the cytoskeletal proteins such as those from the paraflagellar rod and the tubulins, which are both markedly dephosphorylated. Detailed analysis of the signaling cascades triggered upon T. cruzi binding to extracellular matrix (ECM) proteins revealed the involvement of the MAPK/ERK pathway in this event. At the C-terminus, the conserved FLY sequence is a cytokeratin-binding domain and is involved in augmented host cell invasion in vitro and high levels of parasitemia in vivo. FLY, which is associated to tissue tropism and preferentially binds to the heart vasculature may somehow be correlated with the severe cardiac form, an important clinical manifestation of chronic Chagas' disease.

  Trypanosoma cruzi, variant surface glycoprotein, Gp85 Glycoprotein, Parasite Invasion, tissue tropism, Treg Cell

  NCBI PubMed ID: 24264245
  Publication DOI: 10.1007/978-94-007-7305-9_7
  Journal NLM ID: 0316571
  Publisher: New York: Springer
  Correspondence: mjmalves@iq.usp.br
  Institutions: Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil
  
   
  
  Trypanosoma cruzi
  CSDB ID 7332 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

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

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

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

  NCBI PubMed ID: 28748758
  Publication DOI: 10.2174/0929867324666170727110801
  Journal NLM ID: 9440157
  Publisher: Saif Zone, Sharjah, U.A.E.: Bentham Science Publishers
  Correspondence: carronal@usp.br
  Institutions: School of Pharmaceutical Sciences of Ribeirão Preto - University of São Paulo, São Paulo, Brazil
  
   
  
  Leishmania major
  CSDB ID 8207 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycosphingolipid, glycosylinositolphosphoceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_1394182,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 7126
  Toledo MS, Levery SB, Bennion B, Guimaraes LL, Castle SA, Lindsey R, Momany M, Park C, Straus AH, Takahashi HK "Analysis of glycosylinositol phosphorylceramides expressed by the opportunistic mycopathogen Aspergillus fumigatus" - Journal of Lipid Research 48(8) (2007) 1801-1824
  

  Acidic glycosphingolipid components were extracted from the opportunistic mycopathogen Aspergillus fumigatus and identified as inositol phosphorylceramide and glycosylinositol phosphorylceramides (GIPCs). Using nuclear magnetic resonance sppectroscopy, mass spectrometry, and other techniques, the structures of six major components were elucidated as Ins-P-Cer (Af-0), Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-2), Manp(α1→2)Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-3a), Manp(α1→3)[Galf(β1→6)]Manp(α1→2)-Ins-P-Cer (Af-3b), Manp(α1→2)-Manp(α1→3)[Galf(β1→6)]Manp(α1→2)Ins-P-Cer (Af-4), and Manp(α1→3)Manp(α1→6)GlcpN(α1→2)Ins-P-Cer (Af-3c) (where Ins = myo-inositol and P = phosphodiester). A minor A. fumigatus GIPC was also identified as the N-acetylated version of Af-3c (Af-3c*), which suggests that formation of the GlcNα1→2Ins linkage may proceed by a two-step process, similar to the GlcNα1→6Ins linkage in glycosylphosphatidylinositol (GPI) anchors (transfer of GlcNAc, followed by enzymatic de-N-acetylation). The glycosylinositol of Af-3b, which bears a distinctive branching Galf(β1→6) residue, is identical to that of a GIPC isolated previously from the dimorphic mycopathogen Paracoccidioides brasiliensis (designated Pb-3), but components Af-3a and Af-4 have novel structures. Overlay immunostaining of A. fumigatus GIPCs separated on thin-layer chromatograms was used to assess their reactivity against sera from a patient with aspergillosis and against a murine monoclonal antibody (MEST-1) shown previously to react with the Galf(β1→6) residue in Pb-3. These results are discussed in relation to pathogenicity and potential approaches to the immunodiagnosis of A. fumigatus.

  monoclonal antibody, NMR spectroscopy, mass spectrometry, galactofuranose, glycolipid, Electrospray Ionization, fungus, sphingolipid, ion trap

  NCBI PubMed ID: 17488996
  Publication DOI: 10.1194/jlr.M700149-JLR200
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Levery SB , Takahashi HK
  Institutions: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, Brazil, Department of Chemistry, University of New Hampshire, Durham, North Carolina, USA, Department of Plant Biology, University of Georgia, Athens, Georgia, USA
  Methods: 13C NMR, 1H NMR, methylation, NMR-2D, GC-MS, ESI-MS, composition analysis, serological methods, HPLC, ion-exchange chromatography, extraction, CID-MS, HPTLC, ESI-QTOF-MS, HPTLC immunostaining
  
   
  
  Aspergillus fumigatus 9197, Aspergillus fumigatus 237
  CSDB ID 41798 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycosphingolipid, glycosylinositolphosphoceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_1394182,IEDB_140116,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 7126
  Toledo MS, Levery SB, Bennion B, Guimaraes LL, Castle SA, Lindsey R, Momany M, Park C, Straus AH, Takahashi HK "Analysis of glycosylinositol phosphorylceramides expressed by the opportunistic mycopathogen Aspergillus fumigatus" - Journal of Lipid Research 48(8) (2007) 1801-1824
  

  Acidic glycosphingolipid components were extracted from the opportunistic mycopathogen Aspergillus fumigatus and identified as inositol phosphorylceramide and glycosylinositol phosphorylceramides (GIPCs). Using nuclear magnetic resonance sppectroscopy, mass spectrometry, and other techniques, the structures of six major components were elucidated as Ins-P-Cer (Af-0), Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-2), Manp(α1→2)Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-3a), Manp(α1→3)[Galf(β1→6)]Manp(α1→2)-Ins-P-Cer (Af-3b), Manp(α1→2)-Manp(α1→3)[Galf(β1→6)]Manp(α1→2)Ins-P-Cer (Af-4), and Manp(α1→3)Manp(α1→6)GlcpN(α1→2)Ins-P-Cer (Af-3c) (where Ins = myo-inositol and P = phosphodiester). A minor A. fumigatus GIPC was also identified as the N-acetylated version of Af-3c (Af-3c*), which suggests that formation of the GlcNα1→2Ins linkage may proceed by a two-step process, similar to the GlcNα1→6Ins linkage in glycosylphosphatidylinositol (GPI) anchors (transfer of GlcNAc, followed by enzymatic de-N-acetylation). The glycosylinositol of Af-3b, which bears a distinctive branching Galf(β1→6) residue, is identical to that of a GIPC isolated previously from the dimorphic mycopathogen Paracoccidioides brasiliensis (designated Pb-3), but components Af-3a and Af-4 have novel structures. Overlay immunostaining of A. fumigatus GIPCs separated on thin-layer chromatograms was used to assess their reactivity against sera from a patient with aspergillosis and against a murine monoclonal antibody (MEST-1) shown previously to react with the Galf(β1→6) residue in Pb-3. These results are discussed in relation to pathogenicity and potential approaches to the immunodiagnosis of A. fumigatus.

  monoclonal antibody, NMR spectroscopy, mass spectrometry, galactofuranose, glycolipid, Electrospray Ionization, fungus, sphingolipid, ion trap

  NCBI PubMed ID: 17488996
  Publication DOI: 10.1194/jlr.M700149-JLR200
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Levery SB , Takahashi HK
  Institutions: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, Brazil, Department of Chemistry, University of New Hampshire, Durham, North Carolina, USA, Department of Plant Biology, University of Georgia, Athens, Georgia, USA
  Methods: 13C NMR, 1H NMR, methylation, NMR-2D, GC-MS, ESI-MS, composition analysis, serological methods, HPLC, ion-exchange chromatography, extraction, CID-MS, HPTLC, ESI-QTOF-MS, HPTLC immunostaining
  
   
  
  Aspergillus fumigatus 237
  CSDB ID 42014 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycosphingolipid, glycosylinositolphosphoceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_1394182,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 7126
  Toledo MS, Levery SB, Bennion B, Guimaraes LL, Castle SA, Lindsey R, Momany M, Park C, Straus AH, Takahashi HK "Analysis of glycosylinositol phosphorylceramides expressed by the opportunistic mycopathogen Aspergillus fumigatus" - Journal of Lipid Research 48(8) (2007) 1801-1824
  

  Acidic glycosphingolipid components were extracted from the opportunistic mycopathogen Aspergillus fumigatus and identified as inositol phosphorylceramide and glycosylinositol phosphorylceramides (GIPCs). Using nuclear magnetic resonance sppectroscopy, mass spectrometry, and other techniques, the structures of six major components were elucidated as Ins-P-Cer (Af-0), Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-2), Manp(α1→2)Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-3a), Manp(α1→3)[Galf(β1→6)]Manp(α1→2)-Ins-P-Cer (Af-3b), Manp(α1→2)-Manp(α1→3)[Galf(β1→6)]Manp(α1→2)Ins-P-Cer (Af-4), and Manp(α1→3)Manp(α1→6)GlcpN(α1→2)Ins-P-Cer (Af-3c) (where Ins = myo-inositol and P = phosphodiester). A minor A. fumigatus GIPC was also identified as the N-acetylated version of Af-3c (Af-3c*), which suggests that formation of the GlcNα1→2Ins linkage may proceed by a two-step process, similar to the GlcNα1→6Ins linkage in glycosylphosphatidylinositol (GPI) anchors (transfer of GlcNAc, followed by enzymatic de-N-acetylation). The glycosylinositol of Af-3b, which bears a distinctive branching Galf(β1→6) residue, is identical to that of a GIPC isolated previously from the dimorphic mycopathogen Paracoccidioides brasiliensis (designated Pb-3), but components Af-3a and Af-4 have novel structures. Overlay immunostaining of A. fumigatus GIPCs separated on thin-layer chromatograms was used to assess their reactivity against sera from a patient with aspergillosis and against a murine monoclonal antibody (MEST-1) shown previously to react with the Galf(β1→6) residue in Pb-3. These results are discussed in relation to pathogenicity and potential approaches to the immunodiagnosis of A. fumigatus.

  monoclonal antibody, NMR spectroscopy, mass spectrometry, galactofuranose, glycolipid, Electrospray Ionization, fungus, sphingolipid, ion trap

  NCBI PubMed ID: 17488996
  Publication DOI: 10.1194/jlr.M700149-JLR200
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Levery SB , Takahashi HK
  Institutions: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, Brazil, Department of Chemistry, University of New Hampshire, Durham, North Carolina, USA, Department of Plant Biology, University of Georgia, Athens, Georgia, USA
  Methods: 13C NMR, 1H NMR, methylation, NMR-2D, GC-MS, ESI-MS, composition analysis, serological methods, HPLC, ion-exchange chromatography, extraction, CID-MS, HPTLC, ESI-QTOF-MS, HPTLC immunostaining
  
   
  
  Aspergillus fumigatus 9197, Paracoccidioides brasiliensis
  CSDB ID 42015 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycosphingolipid, glycosylinositolphosphoceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_1394182,IEDB_140116,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 7126
  Toledo MS, Levery SB, Bennion B, Guimaraes LL, Castle SA, Lindsey R, Momany M, Park C, Straus AH, Takahashi HK "Analysis of glycosylinositol phosphorylceramides expressed by the opportunistic mycopathogen Aspergillus fumigatus" - Journal of Lipid Research 48(8) (2007) 1801-1824
  

  Acidic glycosphingolipid components were extracted from the opportunistic mycopathogen Aspergillus fumigatus and identified as inositol phosphorylceramide and glycosylinositol phosphorylceramides (GIPCs). Using nuclear magnetic resonance sppectroscopy, mass spectrometry, and other techniques, the structures of six major components were elucidated as Ins-P-Cer (Af-0), Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-2), Manp(α1→2)Manp(α1→3)Manp(α1→2)Ins-P-Cer (Af-3a), Manp(α1→3)[Galf(β1→6)]Manp(α1→2)-Ins-P-Cer (Af-3b), Manp(α1→2)-Manp(α1→3)[Galf(β1→6)]Manp(α1→2)Ins-P-Cer (Af-4), and Manp(α1→3)Manp(α1→6)GlcpN(α1→2)Ins-P-Cer (Af-3c) (where Ins = myo-inositol and P = phosphodiester). A minor A. fumigatus GIPC was also identified as the N-acetylated version of Af-3c (Af-3c*), which suggests that formation of the GlcNα1→2Ins linkage may proceed by a two-step process, similar to the GlcNα1→6Ins linkage in glycosylphosphatidylinositol (GPI) anchors (transfer of GlcNAc, followed by enzymatic de-N-acetylation). The glycosylinositol of Af-3b, which bears a distinctive branching Galf(β1→6) residue, is identical to that of a GIPC isolated previously from the dimorphic mycopathogen Paracoccidioides brasiliensis (designated Pb-3), but components Af-3a and Af-4 have novel structures. Overlay immunostaining of A. fumigatus GIPCs separated on thin-layer chromatograms was used to assess their reactivity against sera from a patient with aspergillosis and against a murine monoclonal antibody (MEST-1) shown previously to react with the Galf(β1→6) residue in Pb-3. These results are discussed in relation to pathogenicity and potential approaches to the immunodiagnosis of A. fumigatus.

  monoclonal antibody, NMR spectroscopy, mass spectrometry, galactofuranose, glycolipid, Electrospray Ionization, fungus, sphingolipid, ion trap

  NCBI PubMed ID: 17488996
  Publication DOI: 10.1194/jlr.M700149-JLR200
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Levery SB , Takahashi HK
  Institutions: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, Brazil, Department of Chemistry, University of New Hampshire, Durham, North Carolina, USA, Department of Plant Biology, University of Georgia, Athens, Georgia, USA
  Methods: 13C NMR, 1H NMR, methylation, NMR-2D, GC-MS, ESI-MS, composition analysis, serological methods, HPLC, ion-exchange chromatography, extraction, CID-MS, HPTLC, ESI-QTOF-MS, HPTLC immunostaining
  
   
  
  Aspergillus fumigatus 9197
  CSDB ID 42016 (all data & tools)