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
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: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130695,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_167835,IEDB_174840,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 6628
  Fankhauser C, Homans SW, Thomas-Oates JE, McConville MJ, Desponds C, Conzelmann A, Ferguson MAJ "Structures of glycosylphosphatidylinositol membrane anchors from Saccharomyces cerevisiae" - Journal of Biological Chemistry 268 (1993) 26365-26374
  

  Metabolic labeling studies suggest that Saccharomyces cerevisiae contains many glycoproteins that are anchored in the lipid bilayer by glycosylphosphatidylinositol membrane anchors. Membrane anchors were purified from a crude yeast membrane protein fraction and analyzed by two-dimensional 1H-1H NMR, fast atom bombardment-mass spectrometry, compositional and methylation linkage analyses, as well as chemical and enzymatic modifications. The yeast glycosylphosphatidylinositol anchors consist of the following structures: ethanolamine-PO4-6(R-2)Man(α1-2)Man(α1-6)Man(α1-4)Glc-NH2(α1-6)myo-inositol-1-PO4-lipid, where R is mainly Man(α1- (80%) with some Man(α1-2)Man(α1- (15%) and Man(α1-3)Man(α1- (5%). The core region of the yeast anchors (ethanolamine-PO4-6Man α 1-2Man α 1-6Man α 1-4GlcNH2 α 1-6myo-inositol-1-PO4) is identical to the conserved core region found in glycosylphosphatidylinositol anchors from protozoa and mammals. The lipid moieties of the total yeast glycosylphosphatidylinositol anchors are mainly ceramides, consisting mostly of C18:0 phytosphingosine and C26:0 fatty acid. However, the lipid moiety of the glycosylphosphatidylinositol anchor of the purified ggp125 protein is a lyso- or diacylglycerol, containing C26:0 fatty acids. This suggests that yeast adds different lipid components to the glycosylphosphatidylinositol anchors of different proteins.

  NCBI PubMed ID: 8253761
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 136855 (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_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• 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: 8373346
  Publication DOI: 10.1042/bj2940305
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Institutions: Department of Biochemistry, University of Dundee, U.K., Department of Biochemistry, University of Dundee, U.K
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 106325 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycophospholipid, glycosylphosphatidylinositol (GPI)
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141181,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7138
  Pittet M1, Conzelmann A "Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae" - Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids 1771(3) (2007) 405-420
  

  Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at the plasma membrane, a majority of them gets further processed and is integrated into the cell wall by a covalent attachment to cell wall glucans. The GPI biosynthetic pathway is necessary for growth and survival of yeast cells. The GPI lipids are synthesized in the ER and added onto proteins by a pathway comprising 12 steps, carried out by 23 gene products, 19 of which are essential. Some of the estimated 60 GPI proteins predicted from the genome sequence serve enzymatic functions required for the biosynthesis and the continuous shape adaptations of the cell wall, others seem to be structural elements of the cell wall and yet others mediate cell adhesion. Because of its genetic tractability S. cerevisiae is an attractive model organism not only for studying GPI biosynthesis in general, but equally for investigating the intracellular transport of GPI proteins and the peculiar role of GPI anchoring in the elaboration of fungal cell walls.

  biosynthesis, cell wall, ceramide, Glycosylphosphatidylinositol, Saccharomyces cerevisiae, Lipid remodeling

  NCBI PubMed ID: 16859984
  Publication DOI: 10.1016/j.bbalip.2006.05.015
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: andreas.conzelmann@unifr.ch (Andreas Conzelmann)
  Institutions: Department of Medicine, Division of Biochemistry, Fribourg, Switzerland
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 41811 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: glycophospholipid, glycosylphosphatidylinositol (GPI)
Contained glycoepitopes: IEDB_1068707,IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141181,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_158638,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_176772,IEDB_474450,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7138
  Pittet M1, Conzelmann A "Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae" - Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids 1771(3) (2007) 405-420
  

  Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at the plasma membrane, a majority of them gets further processed and is integrated into the cell wall by a covalent attachment to cell wall glucans. The GPI biosynthetic pathway is necessary for growth and survival of yeast cells. The GPI lipids are synthesized in the ER and added onto proteins by a pathway comprising 12 steps, carried out by 23 gene products, 19 of which are essential. Some of the estimated 60 GPI proteins predicted from the genome sequence serve enzymatic functions required for the biosynthesis and the continuous shape adaptations of the cell wall, others seem to be structural elements of the cell wall and yet others mediate cell adhesion. Because of its genetic tractability S. cerevisiae is an attractive model organism not only for studying GPI biosynthesis in general, but equally for investigating the intracellular transport of GPI proteins and the peculiar role of GPI anchoring in the elaboration of fungal cell walls.

  biosynthesis, cell wall, ceramide, Glycosylphosphatidylinositol, Saccharomyces cerevisiae, Lipid remodeling

  NCBI PubMed ID: 16859984
  Publication DOI: 10.1016/j.bbalip.2006.05.015
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: andreas.conzelmann@unifr.ch (Andreas Conzelmann)
  Institutions: Department of Medicine, Division of Biochemistry, Fribourg, Switzerland
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 42214 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: ceramide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72

• Article ID: 7294
  Haak D, Gable K, Beeler T, Dunn T "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p" - Journal of Biological Chemistry 272(47) (1997) 29704-29710
  

  The Saccharomyces cerevisiae SCS7 and SUR2 genes are members of a gene family that encodes enzymes that desaturate or hydroxylate lipids. Sur2p is required for the hydroxylation of C-4 of the sphingoid moiety of ceramide, and Scs7p is required for the hydroxylation of the very long chain fatty acid. Neither SCS7 nor SUR2 are essential for growth, and lack of the Scs7p- or Sur2p-dependent hydroxylation does not prevent the synthesis of mannosyldiinositolphosphorylceramide, the mature sphingolipid found in yeast. Deletion of either gene suppresses the Ca2+-sensitive phenotype of csg2Delta mutants, which arises from overaccumulation of inositolphosphorylceramide due to a defect in sphingolipid mannosylation. Characterization of scs7 and sur2 mutants is expected to provide insight into the function of ceramide hydroxylation.

  ceramide, hydroxylation, desaturation

  NCBI PubMed ID: 9368039
  Publication DOI: 10.1074/jbc.272.47.29704
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, USA
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae (Δsur2 mutant), Saccharomyces cerevisiae (Δsur2Δscs7 mutant)
  CSDB ID 43536 (all data & tools)
• Article ID: 7295
  Uemura S, Kihara A, Inokuchi J, Igarashi Y "Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p" - Journal of Biological Chemistry 278(46) (2003) 45049-45055
  

  Csg1p and Csg2p have been shown to be involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. YBR161w, termed CSH1 here, encodes a protein that exhibits a strong similarity to Csg1p. To examine whether Csh1p also functions in MIPC synthesis, we performed a [3H]dihydrosphingosine labeling experiment. Deltacsg1 cells exhibited only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the Deltacsg1 Deltacsh1 double deletion mutant exhibited a total loss. These results indicated that Csg1p and Csh1p have redundant functions in MIPC synthesis. Analyses using Deltacsg1 and Deltacsh1 cells in the Deltaipt1, Deltasur2, or Deltascs7 genetic background demonstrated that Csh1p has a different substrate specificity from Csg1p. We also revealed that Csg2p interacts with both Csg1p and Csh1p. Deletion of the CSG2 gene reduced the Csg1p activity and abolished the Csh1p activity. These results suggested that two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist.

  ceramide, mannosylinositol phosphorylceramide

  NCBI PubMed ID: 12954640
  Publication DOI: 10.1074/jbc.M305498200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: yigarash@pharm.hokudai.ac.jp
  Institutions: Department of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Japan
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, immunoblotting, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY05, Saccharomyces cerevisiae SUY41, Saccharomyces cerevisiae SUY42
  CSDB ID 45001 (all data & tools)
• Article ID: 8260
  Uemura S, Shishido F, Tani M, Mochizuki T, Abe F, Inokuchi J "Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae" - Journal of Lipid Research 55(7) (2014) 1343-1356
  

  In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group.

  glycolipids, hydroxyl group, sphingolipids, Saccharomyces cerevisiae, yeast, lipid rafts, fluorescence recovery after photobleaching, membranes fluidity

  NCBI PubMed ID: 24875539
  Publication DOI: 10.1194/jlr.M048637
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Uemura S
  Institutions: Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan, Division of Glycopathology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan, Department of Chemistry, Kyushu University, Fukuoka, Japan, Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan
  Methods: SDS-PAGE, DNA techniques, TLC, alkaline hydrolysis, immunoblotting, extraction, fluorescence spectroscopy
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY12 (Δsur2 mutant), Saccharomyces cerevisiae SUY16 (Δscs7 mutant), Saccharomyces cerevisiae SUY359 (Δsur2Δscs7 mutant)
  CSDB ID 46608 (all data & tools)

Show legend Show as text

Structure type: monomer
Trivial name: sphingolipid
Compound class: glycolipid, ceramide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72

• Article ID: 7294
  Haak D, Gable K, Beeler T, Dunn T "Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p" - Journal of Biological Chemistry 272(47) (1997) 29704-29710
  

  The Saccharomyces cerevisiae SCS7 and SUR2 genes are members of a gene family that encodes enzymes that desaturate or hydroxylate lipids. Sur2p is required for the hydroxylation of C-4 of the sphingoid moiety of ceramide, and Scs7p is required for the hydroxylation of the very long chain fatty acid. Neither SCS7 nor SUR2 are essential for growth, and lack of the Scs7p- or Sur2p-dependent hydroxylation does not prevent the synthesis of mannosyldiinositolphosphorylceramide, the mature sphingolipid found in yeast. Deletion of either gene suppresses the Ca2+-sensitive phenotype of csg2Delta mutants, which arises from overaccumulation of inositolphosphorylceramide due to a defect in sphingolipid mannosylation. Characterization of scs7 and sur2 mutants is expected to provide insight into the function of ceramide hydroxylation.

  ceramide, hydroxylation, desaturation

  NCBI PubMed ID: 9368039
  Publication DOI: 10.1074/jbc.272.47.29704
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, USA
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae (Δscs mutant)
  CSDB ID 43538 (all data & tools)
• Article ID: 7295
  Uemura S, Kihara A, Inokuchi J, Igarashi Y "Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p" - Journal of Biological Chemistry 278(46) (2003) 45049-45055
  

  Csg1p and Csg2p have been shown to be involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. YBR161w, termed CSH1 here, encodes a protein that exhibits a strong similarity to Csg1p. To examine whether Csh1p also functions in MIPC synthesis, we performed a [3H]dihydrosphingosine labeling experiment. Deltacsg1 cells exhibited only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the Deltacsg1 Deltacsh1 double deletion mutant exhibited a total loss. These results indicated that Csg1p and Csh1p have redundant functions in MIPC synthesis. Analyses using Deltacsg1 and Deltacsh1 cells in the Deltaipt1, Deltasur2, or Deltascs7 genetic background demonstrated that Csh1p has a different substrate specificity from Csg1p. We also revealed that Csg2p interacts with both Csg1p and Csh1p. Deletion of the CSG2 gene reduced the Csg1p activity and abolished the Csh1p activity. These results suggested that two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist.

  ceramide, mannosylinositol phosphorylceramide

  NCBI PubMed ID: 12954640
  Publication DOI: 10.1074/jbc.M305498200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: yigarash@pharm.hokudai.ac.jp
  Institutions: Department of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Japan
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, immunoblotting, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY05, Saccharomyces cerevisiae SUY41
  CSDB ID 45003 (all data & tools)
• Article ID: 8001
  Guan XL, Wenk MR "Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae" - Yeast 23(6) (2006) 465-477
  

  Lipids are rapidly moving to centre stage in many fields of biological sciences. Lipidomics, the systems-level scale analysis of lipids and their interacting factors, is thus an emerging field which holds great promise for drug and biomarker discovery. Here we present a mass spectrometry-based approach for profiling of polar lipids, in particular phospholipids and sphingolipids, in Saccharomyces cerevisiae. The first step includes semi-quantitative surveys of lipids in an untargeted fashion, which is particularly powerful for detection of changes that cannot easily be anticipated. This leads to the identification of ions with increased or decreased signal intensities. Comprehensive theoretical calculation of the masses of yeast phospholipid and sphingolipid molecular species, based on fatty acyl and headgroup heterogeneity, is next used to tentatively assign ions of interest. Subsequent targeted analysis using tandem mass spectrometry allows for characterization and quantification of phospholipids and sphingolipids. Given the high degree of conservation in pathways of lipid metabolism between different organisms, it can be expected that this method will lead to the discovery of novel enzymatic activities and modulators of known ones, particularly when used in combination with genetic and chemogenetic libraries and screens. We validated the method using the EUROSCARF library of non-essential deletion mutants. Mutants of SCS7, a lipid hydroxylase, and SLC1, a putative acyl transferase with unknown substrate specificity, were profiled for their phospholipid and sphingolipid content. The observed changes in lipid profiles are consistent with previous observations and extend our knowledge on in vivo substrate use under permissive growth conditions.

  mass spectrometry, phospholipid, lipidomics, sphingolipid, S. cerevisiae

  NCBI PubMed ID: 16652392
  Publication DOI: 10.1002/yea.1362
  Journal NLM ID: 8607637
  Publisher: Chichester, Wiley
  Correspondence: Wenk MR
  Institutions: Department of Biochemistry and Department of Biological Sciences, National University of Singapore, Singapore
  Methods: extraction, ESI-QTOF-MS/MS, cell growth
  
   
  
  Saccharomyces cerevisiae BY4741, Saccharomyces cerevisiae (Δslc1 mutant), Saccharomyces cerevisiae (Δscs7 mutant)
  CSDB ID 45511 (all data & tools)
• Article ID: 8260
  Uemura S, Shishido F, Tani M, Mochizuki T, Abe F, Inokuchi J "Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae" - Journal of Lipid Research 55(7) (2014) 1343-1356
  

  In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group.

  glycolipids, hydroxyl group, sphingolipids, Saccharomyces cerevisiae, yeast, lipid rafts, fluorescence recovery after photobleaching, membranes fluidity

  NCBI PubMed ID: 24875539
  Publication DOI: 10.1194/jlr.M048637
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Uemura S
  Institutions: Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan, Division of Glycopathology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan, Department of Chemistry, Kyushu University, Fukuoka, Japan, Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan
  Methods: SDS-PAGE, DNA techniques, TLC, alkaline hydrolysis, immunoblotting, extraction, fluorescence spectroscopy
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY16 (Δscs7 mutant)
  CSDB ID 46610 (all data & tools)
• Article ID: 9388
  Moreno-Velásquez SD, Tint SH, Del Olmo Toledo V, Torsin S, De S, Pérez JC "The regulatory proteins Rtg1/3 govern sphingolipid homeostasis in the human-associated yeast Candida albicans" - Cell Reports 30(3) (2020) 620-629
  

  Integrating nutrient sensing with the synthesis of complex molecules is a central feature of metabolism. Yet the regulatory mechanisms underlying such integration are often unknown. Here, we establish that the transcription regulators Rtg1/3 are key determinants of sphingolipid homeostasis in the human fungal pathogen Candida albicans. Quantitative analysis of the C. albicans lipidome reveals Rtg1/3-dependent alterations in all complex sphingolipids and their precursors, ceramides. Mutations in the regulators render the fungus susceptible to myriocin, a sphingolipid synthesis inhibitor. Rtg1/3 exert control on the expression of several enzymes involved in the synthesis of sphingolipids' building blocks, and the regulators are activated upon engulfment of C. albicans cells by human neutrophils. We demonstrate that Rtg1p and Rtg3p are regulated at two levels, one in response to sphingolipids and the other by the nutrient sensor TOR. Our findings, therefore, indicate that the Rtg1/3 system integrates nutrient sensing into the synthesis of complex lipids.

  Candida albicans, sphingolipids, yeast, Rtg1, Rtg3, TOR

  NCBI PubMed ID: 31968241
  Publication DOI: 10.1016/j.celrep.2019.12.022
  Journal NLM ID: 101573691
  Publisher: Cambridge, MA: Cell Press
  Correspondence: christian.perez@uni-wuerzburg.de
  Institutions: Interdisciplinary Center for Clinical Research, University Hospital Würzburg, Würzburg, Germany, Institute for Molecular Infection Biology, University of Würzburg, Würzburg, Germany, USAID Challenge TB Project, Yangon, Myanmar
  Methods: DNA techniques, microscopy
  
   
  
  Candida albicans
  CSDB ID 51152 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: ceramide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72

• Article ID: 7295
  Uemura S, Kihara A, Inokuchi J, Igarashi Y "Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p" - Journal of Biological Chemistry 278(46) (2003) 45049-45055
  

  Csg1p and Csg2p have been shown to be involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. YBR161w, termed CSH1 here, encodes a protein that exhibits a strong similarity to Csg1p. To examine whether Csh1p also functions in MIPC synthesis, we performed a [3H]dihydrosphingosine labeling experiment. Deltacsg1 cells exhibited only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the Deltacsg1 Deltacsh1 double deletion mutant exhibited a total loss. These results indicated that Csg1p and Csh1p have redundant functions in MIPC synthesis. Analyses using Deltacsg1 and Deltacsh1 cells in the Deltaipt1, Deltasur2, or Deltascs7 genetic background demonstrated that Csh1p has a different substrate specificity from Csg1p. We also revealed that Csg2p interacts with both Csg1p and Csh1p. Deletion of the CSG2 gene reduced the Csg1p activity and abolished the Csh1p activity. These results suggested that two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist.

  ceramide, mannosylinositol phosphorylceramide

  NCBI PubMed ID: 12954640
  Publication DOI: 10.1074/jbc.M305498200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: yigarash@pharm.hokudai.ac.jp
  Institutions: Department of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Japan
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, immunoblotting, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY05, Saccharomyces cerevisiae SUY41
  CSDB ID 45006 (all data & tools)
• Article ID: 8260
  Uemura S, Shishido F, Tani M, Mochizuki T, Abe F, Inokuchi J "Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae" - Journal of Lipid Research 55(7) (2014) 1343-1356
  

  In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group.

  glycolipids, hydroxyl group, sphingolipids, Saccharomyces cerevisiae, yeast, lipid rafts, fluorescence recovery after photobleaching, membranes fluidity

  NCBI PubMed ID: 24875539
  Publication DOI: 10.1194/jlr.M048637
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Uemura S
  Institutions: Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan, Division of Glycopathology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan, Department of Chemistry, Kyushu University, Fukuoka, Japan, Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan
  Methods: SDS-PAGE, DNA techniques, TLC, alkaline hydrolysis, immunoblotting, extraction, fluorescence spectroscopy
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY12 (Δsur2 mutant), Saccharomyces cerevisiae SUY16 (Δscs7 mutant), Saccharomyces cerevisiae SUY359 (Δsur2Δscs7 mutant)
  CSDB ID 46613 (all data & tools)

Show legend Show as text

Structure type: monomer
Trivial name: sphingolipid
Compound class: glycolipid, ceramide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72

• Article ID: 7295
  Uemura S, Kihara A, Inokuchi J, Igarashi Y "Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p" - Journal of Biological Chemistry 278(46) (2003) 45049-45055
  

  Csg1p and Csg2p have been shown to be involved in the synthesis of mannosylinositol phosphorylceramide (MIPC) from inositol phosphorylceramide. YBR161w, termed CSH1 here, encodes a protein that exhibits a strong similarity to Csg1p. To examine whether Csh1p also functions in MIPC synthesis, we performed a [3H]dihydrosphingosine labeling experiment. Deltacsg1 cells exhibited only a reduction in the synthesis of mannosylated sphingolipids compared with wild-type cells, whereas the Deltacsg1 Deltacsh1 double deletion mutant exhibited a total loss. These results indicated that Csg1p and Csh1p have redundant functions in MIPC synthesis. Analyses using Deltacsg1 and Deltacsh1 cells in the Deltaipt1, Deltasur2, or Deltascs7 genetic background demonstrated that Csh1p has a different substrate specificity from Csg1p. We also revealed that Csg2p interacts with both Csg1p and Csh1p. Deletion of the CSG2 gene reduced the Csg1p activity and abolished the Csh1p activity. These results suggested that two distinct inositol phosphorylceramide mannosyltransferase complexes, Csg1p-Csg2p and Csh1p-Csg2p, exist.

  ceramide, mannosylinositol phosphorylceramide

  NCBI PubMed ID: 12954640
  Publication DOI: 10.1074/jbc.M305498200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: yigarash@pharm.hokudai.ac.jp
  Institutions: Department of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Japan
  Methods: DNA techniques, TLC, methanolysis, alkaline hydrolysis, immunoblotting, extraction, cell growth
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY05, Saccharomyces cerevisiae SUY41
  CSDB ID 45008 (all data & tools)
• Article ID: 8001
  Guan XL, Wenk MR "Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae" - Yeast 23(6) (2006) 465-477
  

  Lipids are rapidly moving to centre stage in many fields of biological sciences. Lipidomics, the systems-level scale analysis of lipids and their interacting factors, is thus an emerging field which holds great promise for drug and biomarker discovery. Here we present a mass spectrometry-based approach for profiling of polar lipids, in particular phospholipids and sphingolipids, in Saccharomyces cerevisiae. The first step includes semi-quantitative surveys of lipids in an untargeted fashion, which is particularly powerful for detection of changes that cannot easily be anticipated. This leads to the identification of ions with increased or decreased signal intensities. Comprehensive theoretical calculation of the masses of yeast phospholipid and sphingolipid molecular species, based on fatty acyl and headgroup heterogeneity, is next used to tentatively assign ions of interest. Subsequent targeted analysis using tandem mass spectrometry allows for characterization and quantification of phospholipids and sphingolipids. Given the high degree of conservation in pathways of lipid metabolism between different organisms, it can be expected that this method will lead to the discovery of novel enzymatic activities and modulators of known ones, particularly when used in combination with genetic and chemogenetic libraries and screens. We validated the method using the EUROSCARF library of non-essential deletion mutants. Mutants of SCS7, a lipid hydroxylase, and SLC1, a putative acyl transferase with unknown substrate specificity, were profiled for their phospholipid and sphingolipid content. The observed changes in lipid profiles are consistent with previous observations and extend our knowledge on in vivo substrate use under permissive growth conditions.

  mass spectrometry, phospholipid, lipidomics, sphingolipid, S. cerevisiae

  NCBI PubMed ID: 16652392
  Publication DOI: 10.1002/yea.1362
  Journal NLM ID: 8607637
  Publisher: Chichester, Wiley
  Correspondence: Wenk MR
  Institutions: Department of Biochemistry and Department of Biological Sciences, National University of Singapore, Singapore
  Methods: extraction, ESI-QTOF-MS/MS, cell growth
  
   
  
  Saccharomyces cerevisiae BY4741
  CSDB ID 45509 (all data & tools)
• Article ID: 8260
  Uemura S, Shishido F, Tani M, Mochizuki T, Abe F, Inokuchi J "Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae" - Journal of Lipid Research 55(7) (2014) 1343-1356
  

  In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group.

  glycolipids, hydroxyl group, sphingolipids, Saccharomyces cerevisiae, yeast, lipid rafts, fluorescence recovery after photobleaching, membranes fluidity

  NCBI PubMed ID: 24875539
  Publication DOI: 10.1194/jlr.M048637
  Journal NLM ID: 0376606
  Publisher: ASBMB
  Correspondence: Uemura S
  Institutions: Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan, Division of Glycopathology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, Sendai, Japan, Department of Chemistry, Kyushu University, Fukuoka, Japan, Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan
  Methods: SDS-PAGE, DNA techniques, TLC, alkaline hydrolysis, immunoblotting, extraction, fluorescence spectroscopy
  
   
  
  Saccharomyces cerevisiae KA31-1A, Saccharomyces cerevisiae SUY16 (Δscs7 mutant)
  CSDB ID 46615 (all data & tools)