Show legend Show as text

Structure type: oligomer
Trivial name: glucosylceramide CMH)
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_153911,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• 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 Dm28c
  CSDB ID 7263 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: lactosylceramide (CDH)
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_136044,IEDB_137339,IEDB_137472,IEDB_141181,IEDB_141794,IEDB_141817,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_164044,IEDB_174031,IEDB_190606,IEDB_233996,IEDB_604755,IEDB_952460,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_3,SB_5,SB_6,SB_7,SB_88

• 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 Dm28c
  CSDB ID 5477 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GIPL
Compound class: glycoinositolphospholipid
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141181,IEDB_141793,IEDB_141807,IEDB_141817,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_233996,IEDB_474450,IEDB_76933,IEDB_952460,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 dionisii
  CSDB ID 5485 (all data & tools)

Show legend Show as text

Structure type: monomer ; 766.8 [M+H]+
Compound class: ceramide
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 8043
  Oguro Y, Yamazaki H, Takagi M, Takaku H "Antifungal activity of plant defensin AFP1 in Brassica juncea involves the recognition of the methyl residue in glucosylceramide of target pathogen Candida albicans" - Current Genetics 60(2) (2014) 89-97
  

  An antifungal defensin, AFP1, of Brassica juncea inhibits the growth of various microorganisms. The molecular details of this inhibition remain largely unknown. Herein, we reveal that a specific structure of fungal sphingolipid glucosylceramide (GlcCer) is critical for the sensitivity of Candida albicans cells to AFP1. Our results revealed that AFP1 induces plasma membrane permeabilization and the production of reactive oxygen species (ROS) in wild-type C. albicans cells, but not in cells lacking the ninth methyl residue of the GlcCer sphingoid base moiety, which is a characteristic feature of fungi. AFP1-induced ROS production is responsible for its antifungal activity, with a consequent loss of yeast cell viability. These findings suggest that AFP1 specifically recognizes the structural difference of GlcCer for targeting of the fungal pathogens.

  Candida albicans, glucosylceramide, AFP1, defensin, methyl residue

  NCBI PubMed ID: 24253293
  Publication DOI: 10.1007/s00294-013-0416-8
  Journal NLM ID: 8004904
  Publisher: New York, NY: Springer International
  Correspondence: htakaku@nupals.ac.jp
  Institutions: Department of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences, Niigata, Japan
  Methods: DNA techniques, MALDI-TOF MS, extraction
  
   
  
  Candida albicans (Δsld1 mutant)
  CSDB ID 46520 (all data & tools)

Show legend Show as text

Structure type: monomer ; 766.5
Compound class: cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 8215
  Watanabe T, Ito T, Goda HM, Ishibashi Y, Miyamoto T, Ikeda K, Taguchi R, Okino N, Ito M "Sterylglucoside catabolism in Cryptococcus neoformans with endoglycoceramidase-related protein 2 (EGCrP2), the first steryl-β-glucosidase identified in fungi" - Journal of Biological Chemistry 290(2) (2015) 1005-1019
  

  Cryptococcosis is an infectious disease caused by pathogenic fungi, such as Cryptococcus neoformans and Cryptococcus gattii. The ceramide structure (methyl-d18:2/h18:0) of C. neoformans glucosylceramide (GlcCer) is characteristic and strongly related to its pathogenicity. We recently identified endoglycoceramidase-related protein 1 (EGCrP1) as a glucocerebrosidase in C. neoformans and showed that it was involved in the quality control of GlcCer by eliminating immature GlcCer during the synthesis of GlcCer (Ishibashi, Y., Ikeda, K., Sakaguchi, K., Okino, N., Taguchi, R., and Ito, M. (2012) Quality control of fungus-specific glucosylceramide in Cryptococcus neoformans by endoglycoceramidase-related protein 1 (EGCrP1). J. Biol. Chem. 287, 368-381). We herein identified and characterized EGCrP2, a homologue of EGCrP1, as the enzyme responsible for sterylglucoside catabolism in C. neoformans. In contrast to EGCrP1, which is specific to GlcCer, EGCrP2 hydrolyzed various β-glucosides, including GlcCer, cholesteryl-β-glucoside, ergosteryl-β-glucoside, sitosteryl-β-glucoside, and para-nitrophenyl-β-glucoside, but not α-glucosides or β-galactosides, under acidic conditions. Disruption of the EGCrP2 gene (egcrp2) resulted in the accumulation of a glycolipid, the structure of which was determined following purification to ergosteryl-3β-glucoside, a major sterylglucoside in fungi, by mass spectrometric and two-dimensional nuclear magnetic resonance analyses. This glycolipid accumulated in vacuoles and EGCrP2 was detected in vacuole-enriched fraction. These results indicated that EGCrP2 was involved in the catabolism of ergosteryl-β-glucoside in the vacuoles of C. neoformans. Distinct growth arrest, a dysfunction in cell budding, and an abnormal vacuole morphology were detected in the egcrp2-disrupted mutants, suggesting that EGCrP2 may be a promising target for anti-cryptococcal drugs. EGCrP2, classified into glycohydrolase family 5, is the first steryl-β-glucosidase identified as well as a missing link in sterylglucoside metabolism in fungi

  metabolism, glycolipid, fungi, glycosidase, sterol

  NCBI PubMed ID: 25361768
  Publication DOI: 10.1074/jbc.M114.616300
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: makotoi@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Higashi-ku, Japan, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Japan, Institute for Advanced Biosciences, Keio University, Tsuruoka, Japan, Department of Biomedical Sciences, College of Life and Health Sciences, Chubu University, Kasugai-shi, Japan
  Methods: gel filtration, 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, DNA techniques, MALDI-TOF MS, biological assays, HPLC, Southern blotting, extraction, cell growth, protein detection, enzymatic assay, flow cytometry analysis, centrifugation
  
   
  
  Cryptococcus neoformans var. grubii H99 ATCC 208821 (Δegcrp1 mutant)
  CSDB ID 48264 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 8216
  Watanabe T, Ishibashi Y, Ito M "Physiological significance of glycolipid catabolism in Cryptococcus neoformans" - Trends in Glycoscience and Glycotechnology 22(157) (2015) E21-E31
  

  The pathogenic fungus Cryptococcus neoformans causes cryptococcosis, an opportunistic infectious disease resulting in 600,000 deaths per year. The two major glycolipids in C. neoformans are glucosylceramide (GlcCer) with a fungus-specific ceramide (methyl d18 : 2/h18 : 0) and ergosteryl β-glucoside (EG); however, the catabolic pathway of these glycolipids has not yet been uncovered. We found two homologues of endoglycoceramidase (EGCase, EC 3.2.1.123) in C. neoformans, designated Endoglycoceramidase-related Protein 1 and 2 (EGCrP1 and EGCrP2). EGCase hydrolyzes the O-glycosidic linkage between oligosaccharides and ceramides in various glycosphingolipids. However, EGCrP1 and EGCrP2 show completely different specificities; that is, EGCrP1 is a neutral glucocerebrosidase specific to GlcCer, whereas EGCrP2 is an acid β-glucosidase capable of hydrolyzing not only GlcCer but also various β-glucosides, including pNP β-glucoside and EG. Using each disruption mutant of egcrp1 and egcrp2, we elucidated that EGCrP1 plays an integral role in quality control of the fungus-specific GlcCer by eliminating immature GlcCer, which are byproducts of the GlcCer synthesis pathway, whereas EGCrP2 is involved in the catabolism of EG in the vacuoles of C. neoformans. The analysis of egcrp1-disrupted mutants also revealed that the quality control of fungus-specific GlcCer is strongly linked to the formation of the polysaccharide capsule, an important virulence factor. On the other hand, the disruption of EG catabolism resulted in growth arrest, dysfunction in cell budding, and abnormal vacuole morphology. These results indicate that catabolism of two different glycolipids plays different physiological roles in C. neoformans and strongly suggest EGCrP1 and EGCrP2 as targets for anti-cryptococcal drugs with a new mechanism of action

  capsule, Cryptococcus neoformans, sterylglucoside, glycolipid catabolism, glucosylceramide quality control, vacuole

  Publication DOI: 10.4052/tigg.1504.1E
  Journal NLM ID: 9425898
  Correspondence: makotoi@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Higashi-ku, Japan
  Methods: DNA techniques, TLC, ESI-MS/MS, biological assays, HPLC
  
   
  
  Cryptococcus neoformans
  CSDB ID 48268 (all data & tools)

Show legend Show as text

Structure type: monomer ; 744.4
Compound class: glycosphingolipid, cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 8530
  Singh A, Del Poeta M "Sphingolipidomics: an important mechanistic tool for studying fungal pathogens" - Frontiers in Microbiology 7 (2016) ID 501
  

  Sphingolipids form of a unique and complex group of bioactive lipids in fungi. Structurally, sphingolipids of fungi are quite diverse with unique differences in the sphingoid backbone, amide linked fatty acyl chain and the polar head group. Two of the most studied and conserved sphingolipid classes in fungi are the glucosyl- or galactosyl-ceramides and the phosphorylinositol containing phytoceramides. Comprehensive structural characterization and quantification of these lipids is largely based on advanced analytical mass spectrometry based lipidomic methods. While separation of complex lipid mixtures is achieved through high performance liquid chromatography, the soft - electrospray ionization tandem mass spectrometry allows a high sensitivity and selectivity of detection. Herein, we present an overview of lipid extraction, chromatographic separation and mass spectrometry employed in qualitative and quantitative sphingolipidomics in fungi.

  ceramide, sphingolipids, fungal infections, fungi, electrospray ionization tandem mass spectrometry, high performance liquid chromatography

  NCBI PubMed ID: 27148190
  Publication DOI: 10.3389/fmicb.2016.00501
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: Del Poeta M
  Institutions: Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY, USA, Veterans Administration Medical Center, Northport, NY, USA
  
   
  
  Cryptococcus neoformans
  CSDB ID 42750 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: glycolipid, glycosphingolipid
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 8915
  Nimrichter L, Rodrigues ML, Del Poeta M "Exploiting lipids to develop anticryptococcal vaccines" - Current Tropical Medicine Reports 6 (2019) 55-63
  

  Cryptococcus spp. are responsible for life-threatening infections in humans causing mortality rates of 70% in developing countries. Antifungal therapy to combat cryptococcosis is based on the combination of amphotericin B, azoles, and 5-flucytosine. However, treatment failure is frequently triggered by antifungal resistance, drug-drug interactions, and toxicity. New alternatives to prevent cryptococcosis are imperative. Here, we discuss the roles of lipids in the immunological control of the disease caused by Cryptococcus spp. Recently, remarkable advances on immunology of fungal infections have been made and a number of studies indicated the potential of vaccine formulations to combat cryptococcosis. New formulations exploiting virulence regulators and genetically modified attenuated strains have been tested. In this context, lipids have emerged as virulence regulators and immunogens to be explored. Glucosylceramide (GlcCer), sterylglycosides (SGs), and lipid-containing extracellular vesicles have been recently tested in vaccine formulations and their anticryptococcal efficacy was confirmed in vivo. Together, the data discussed here encourage the use of fungal lipids in anticryptococcal vaccinal strategies.

  glucosylceramide, cryptococcosis, antifungal vaccine, immunogenic lipids, sterylglycosides, extracellular vesicles

  Publication DOI: 10.1007/s40475-019-00178-x
  Journal NLM ID: 101625249
  Publisher: Cham, Switzerland: Springer International Publishing AG
  Correspondence: nimrichter@micro.ufrj.br
  Institutions: Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, USA, Veterans Administration Medical Center, Northport, USA, Instituto de Microbiologia Paulo de Góes (IMPG), Departamento de Microbiologia Geral, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Instituto Carlos Chagas, Fundação Oswaldo Cruz (Fiocruz), Curitiba, Brazil, Department of Medicine, Division of Infectious Diseases, Stony Brook University, Stony Brook, USA
  
   
  
  Cryptococcus neoformans (Δsld8 mutant)
  CSDB ID 50138 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: glycolipid, cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_176772,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 9207
  Song J, Liu X, Li R "Sphingolipids: Regulators of azole drug resistance and fungal pathogenicity" - Molecular Microbiology 114(6) (2020) 891-905
  

  In recent years, the role of sphingolipids in pathogenic fungi, in terms of pathogenicity and resistance to azole drugs, has been a rapidly growing field. This review describes evidence about the roles of sphingolipids in azole resistance and fungal virulence. Sphingolipids can serve as signaling molecules that contribute to azole resistance through modulation of the expression of drug efflux pumps. They also contribute to azole resistance by participating in various microbial pathways such as the unfolded protein response (UPR), pH-responsive Rim pathway, and pleiotropic drug resistance (PDR) pathway. In addition, sphingolipid signaling and eisosomes also coordinately regulate sphingolipid biosynthesis in response to azole-induced membrane stress. Sphingolipids are important for fungal virulence, playing roles during growth in hosts under stressful conditions, maintenance of cell wall integrity, biofilm formation, and production of various virulence factors. Finally, we discuss the possibility of exploiting fungal sphingolipids for the development of new therapeutic strategies to treat infections caused by pathogenic fungi.

  sphingolipids, ergosterol, azole resistance, antifungal therapeutic target, fungal pathogenicity

  NCBI PubMed ID: 32767804
  Publication DOI: 10.1111/mmi.14586
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: Song J ; Li R
  Institutions: The Key Laboratory of Biotechnology for Medicinal Plants of Jiangsu Province and School of Life Science, Jiangsu Normal University, Xuzhou, China
  
   
  
  (fungi)
  CSDB ID 51081 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 716.5695 [M+H]+
C₄₀H₇₇NO₉
Trivial name: Glc-Cer
Compound class: glycolipid, glycosphingolipid, cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_141817,IEDB_142488,IEDB_146664,IEDB_151082,IEDB_174031,IEDB_604755,IEDB_952460,IEDB_983931,SB_192,SB_5

• Article ID: 9742
  Inagaki M, Harada Y, Yamada K, Isobe R, Higuchi R, Matsuura H, Itakura Y "Isolation and structure determination of cerebrosides from garlic, the bulbs of Allium sativum L." - Chemical and Pharmaceutical Bulletin 46 (1998) 1153-1156
  

  Five cerebrosides, AS-1-1 (1), AS-1-2 (2), AS-1-3 (3), AS-1-4 (4), and AS-1-5 (5) were obtained from the CHCl_3-MeOH extract of Garlic, the bulbs of Allium sativum L. (Liliaceae). On the basis of spectroscopic results, structures of 1-5 have been elucidated. Compounds 1,2,and 5 were new cerebrosides. Compounds 3 and 4 were identified with the known glucocerebroside soya-cerebroside I and II, respectively, which have been previously obtained from soybean with ionophoretic activity. Positive ion FAB-MS/MS of the (M+Na)^+ ion gave important information on the length of the fatty acyl chain of the ceramide moiety.

  glycosphingolipid, cerebroside, Allium sativum, garlic, FAB-MS/MS

  Journal NLM ID: 0377775
  WWW link: http://ci.nii.ac.jp/naid/110003616995
  Publisher: Pharmaceutical Society Of Japan
  Institutions: Faculty of Pharmaceutical Sciences, Kyushu University, Japan, Institute for OTC Research, Wakunaga Pharmaceutical Co., Ltd., Japan, Department of Industrial Chemistry, Faculty of Engineering, Towa University, Japan
  Methods: 13C NMR, 1H NMR, FAB-MS, FAB-MS/MS, HPLC, melting point determination
  
   
  
  Allium sativum
  CSDB ID 120869 (all data & tools)