CSDB: Search results

Taxonomic group: fungi / Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Basidiomycota (Phylum: Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Basidiomycota)
Organ / tissue: yeast, hypha
Associated disease: infection due to Paracoccidioides brasiliensis [ICD11: XN5UX

]; infection due to Histoplasma capsulatum [ICD11: XN8VH

]; infection due to Aspergillus fumigatus [ICD11: XN5Z7

]; infection due to Sporothrix schenckii [ICD11: XN6GM

]; infection due to Candida [ICD11: XN3CL

]; infection due to Cryptococcus [ICD11: XN69C

]

NCBI PubMed ID: 19722017
Publication DOI: 10.1590/S0001-37652009000300012
Journal NLM ID: 7503280
Publisher: Academia Brasileira De Ciencias
Correspondence: Anita H. Straus <straus.bioq

epm.br>
Institutions: Setor de Imunoquímica de Glicoconjugados, Departamento de Bioquímica Ed. J.L. Prado, São Paulo, Brasil, Departamento de Microbiologia, Imunologia e Parasitologia, São Paulo, Brasil

Recently, glycosphingolipids have been attracting attention due to their role on biological systems as second messengers or modulators of signal transduction, affecting several events, which range from apoptosis to regulation of the cell cycle. In pathogenic fungi, glycolipids are expressed in two classes: neutral monohexosylceramides (glucosyl-or galactosylceramide) and acidic glycosylinositol phosphorylceramides (the latter class carries longer glycan chains). It is worth to mention that monohexosylceramides exhibit significant structural differences in their lipid moieties compared to their mammalian counterparts, whereas the glycosylinositol phosphorylceramides exhibit remarkable structural differences in their carbohydrate moieties in comparison to mammal glycosphingolipids counterpart. We observed that glycosylinositol phosphorylceramides are capable of promoting immune response in infected humans. In addition, inhibiting fungal glycosphingolipid biosynthetic pathways leads to an inhibition of colony formation, spore germination, cell cycle, dimorphism and hyphal growth. Other pathogens, such as trypanosomatids, also present unique glycolipids, which may have an important role for the parasite development and/or disease establishment. Regarding host-pathogen interaction, cell membrane rafts, which are enriched in sphingolipids and sterols, participate in parasite/fungal infection. In this review, it is discussed the different biological roles of (glyco) (sphingo)lipids of pathogenic/opportunistic fungi and trypanosomatids.

glycosphingolipids, leishmania, glycosylinositol phosphorylceramides, inositol phosphorylceramide, membrane rafts, pathogenic fungi

Structure type: monomer
Location inside paper: p.478, p.479, table I
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_137339,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_983931,SB_192,SB_5

Comments, role: review; neutral glycosphingolipids; 2S,3R-configuration of 9-methyl-4,8-sphingadienine (9b1SphdC19) was assumed basing on analogs; GSLs present in mycelium and yeast forms of S. schenckii; GSLs present in hyphae of A. fumigatus and A. nidulans.

Related record ID(s): 41948, 41949, 41950, 41951, 41952, 42158
NCBI Taxonomy refs (TaxIDs): 121759, 5037, 746128, 29908, 162425, 5475, 5206
Show glycosyltransferases

There are 4 chemically distinct structures. Please, select:

$CCCCCCCCCCCCCCCCC(O)C(=O)N[C@@H](COC1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O)[C@H](O)/C=C/CC/C=C(\C)CCCCCCCCC$

SVG MW SMILES 3D mol Ionize

Taxonomic group: fungi / Basidiomycota (Phylum: Basidiomycota)
Associated disease: infection due to Cryptococcus [ICD11: XN69C

]

NCBI PubMed ID: 31671548
Publication DOI: 10.3390/cells8111348
Journal NLM ID: 101600052
Publisher: Basel, Switzerland: MDPI
Correspondence: Lee DJ <danielle.lee2

griffithuni.edu.au>; O'Donnell H <holly.odonnell

griffithuni.edu.au>; Routier FH <Routier.francoise

mh-hannover.de>Tiralongo J <j.tiralongo

griffith.edu.au>; Haselhorst T <t.haselhorst

griffith.edu.au>
Institutions: Institute for Glycomics, Griffith University, Queensland, Australia, Member of Fraunhofer International Consortium for Anti-Infective Research (iCAIR), Hannover, Germany, Department of Clinical Biochemistry OE4340, Hannover Medical School, Hannover, Germany

Invasive fungal infections (IFI) are an increasing threat to the developing world, with fungal spores being ubiquitous and inhaled every day. Some fungal species are commensal organisms that are part of the normal human microbiota, and, as such, do not pose a threat to the immune system. However, when the natural balance of this association is disturbed or the host's immune system is compromised, these fungal pathogens overtake the organism, and cause IFI. To understand the invasiveness of these pathogens and to address the growing problem of IFI, it is essential to identify the cellular processes of the invading organism and their virulence. In this review, we will discuss the prevalence and current options available to treat IFI, including recent reports of drug resistance. Nevertheless, the main focus of this review is to describe the glycobiology of human fungal pathogens and how various components of the fungal cell wall, particularly cell wall polysaccharides and glycoconjugates, are involved in fungal pathogenicity, their biosynthesis and how they can be potentially exploited to develop novel antifungal treatment options. We will specifically describe the nucleotide sugar transporters (NSTs) that are important in fungal survival and suggest that the inhibition of fungal NSTs may potentially be useful to prevent the establishment of fungal infections.

UDP-galactofuranose, Candida, Aspergillus, GDP-mannose, Cryptococcus, nucleotide sugar transporter, immunosuppression, invasive fungal infection, UDP-glucuronic acid, UDP-xylose

Structure type: polymer chemical repeating unit
Location inside paper: Fig. 2, g (i)
Trivial name: glucuronoxylomannan (GXM)
Compound class: CPS, EPS, polysaccharide, glucuronoxylomannan
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_115576,IEDB_130701,IEDB_140116,IEDB_140630,IEDB_144983,IEDB_145668,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_2270799,IEDB_423153,IEDB_76933,IEDB_983930,SB_197,SB_44,SB_67,SB_72

Comments, role: the published polymerization frame was shifted for compatibility with other records

Related record ID(s): 50825
NCBI Taxonomy refs (TaxIDs): 5206
Reference(s) to other database(s): GTC:G42955PN, CCSD:50377, CBank-STR:16613
Show glycosyltransferases

There is only one chemically distinct structure:

*O[C@H]1[C@H](O[C@@H]2OC[C@@H](O)[C@H](O)[C@H]2O)[C@@H](CO)O[C@H](O[C@@H]2[C@H](O[C@@H]3OC[C@@H](O)[C@H](O)[C@H]3O)[C@@H](O[C@H]3[C@H](O)[C@@H](CO)O[C@H](*)[C@H]3O[C@@H]3OC[C@@H](O)[C@H](O)[C@H]3O)O[C@H](CO)[C@H]2O)[C@H]1O[C@@H]1O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]1O

SVG MW SMILES 3D mol Ionize

Taxonomic group: fungi / Basidiomycota (Phylum: Basidiomycota)
Associated disease: infection due to Cryptococcus [ICD11: XN69C

]

NCBI PubMed ID: 31671548
Publication DOI: 10.3390/cells8111348
Journal NLM ID: 101600052
Publisher: Basel, Switzerland: MDPI
Correspondence: Lee DJ <danielle.lee2

griffithuni.edu.au>; O'Donnell H <holly.odonnell

griffithuni.edu.au>; Routier FH <Routier.francoise

mh-hannover.de>Tiralongo J <j.tiralongo

griffith.edu.au>; Haselhorst T <t.haselhorst

UDP-galactofuranose, Candida, Aspergillus, GDP-mannose, Cryptococcus, nucleotide sugar transporter, immunosuppression, invasive fungal infection, UDP-glucuronic acid, UDP-xylose

Structure type: polymer chemical repeating unit
Location inside paper: Fig. 2, g (ii)
Compound class: polysaccharide, galactoxylomannan
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_130701,IEDB_134624,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_144983,IEDB_145668,IEDB_151528,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423153,IEDB_983930,SB_163,SB_165,SB_166,SB_187,SB_195,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88

Related record ID(s): 45073
NCBI Taxonomy refs (TaxIDs): 5206
Reference(s) to other database(s): GTC:G05972QE
Show glycosyltransferases

There is only one chemically distinct structure:

*OC[C@H]1O[C@H](OC[C@H]2O[C@H](OC[C@H]3O[C@H](OC[C@H]4O[C@H](*)[C@H](O)[C@@H](O[C@@H]5O[C@H](CO)[C@H](O[C@H]6O[C@H](CO)[C@@H](O)[C@H](O[C@H]7O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]7O)[C@@H]6O)[C@H](O)[C@H]5O)[C@H]4O)[C@H](O)[C@@H](O)[C@H]3O)[C@H](O)[C@@H](O[C@@H]3O[C@H](CO)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O[C@@H]6OC[C@@H](O)[C@H](O)[C@H]6O)[C@@H]5O)[C@@H]4O[C@@H]4OC[C@@H](O)[C@H](O)[C@H]4O)[C@H](O[C@@H]4O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]4O)[C@H]3O)[C@H]2O)[C@H](O)[C@@H](O)[C@H]1O

SVG MW SMILES 3D mol Ionize

Taxonomic group: fungi / Ascomycota, Basidiomycota, Ascomycota (Phylum: Ascomycota, Basidiomycota, Ascomycota)
Associated disease: infection due to Candida [ICD11: XN3CL

]; infection due to Cryptococcus [ICD11: XN69C

]; infection due to Aspergillus fumigatus [ICD11: XN5Z7

]

NCBI PubMed ID: 30046985
Publication DOI: 10.1007/82_2018_103
Journal NLM ID: 0110513
Publisher: Heidelberg: Springer Verlag
Correspondence: Krumm SA <stefanie.krumm

kcl.ac.uk>; Doores KJ <katie.doores

kcl.ac.uk>
Institutions: Department of Infectious Diseases, King’s College London, 2nd Floor, Borough Wing, Guy’s Hospital, London, UK

Glycosylation is an important post-translational modification that is required for structural and stability purposes and functional roles such as signalling, attachment and shielding. Many human pathogens such as bacteria display an array of carbohydrates on their surface that are non-self to the host; others such as viruses highjack the host-cell machinery and present self-carbohydrates sometimes arranged in a non-self more immunogenic manner. In combination with carrier proteins, these glycan structures can be highly immunogenic. During natural infection, glycan-binding antibodies are often elicited that correlate with long-lasting protection. A great amount of research has been invested in carbohydrate vaccine design to elicit such an immune response, which has led to the development of vaccines against the bacterial pathogens Haemophilus influenzae type b, Streptococcus pneumonia and Neisseria meningitidis. Other vaccines, e.g. against HIV-1, are still in development, but promising progress has been made with the isolation of broadly neutralizing glycan-binding antibodies and the engineering of stable trimeric envelope glycoproteins. Carbohydrate vaccines against other pathogens such as viruses (Dengue, Hepatitis C), parasites (Plasmodium) and fungi (Candida) are at different stages of development. This chapter will discuss the challenges in inducing cross-reactive carbohydrate-targeting antibodies and progress towards carbohydrate vaccines.

vaccines, immune response, Candida, glycans, Plasmodium, Dengue, Hepatitis C

Structure type: structural motif or average structure
Location inside paper: Fig. 1, Candida, Cryptococcus, Aspergillus fumigatus
Compound class: glucan, polysaccharide
Contained glycoepitopes: IEDB_135614,IEDB_1397514,IEDB_141806,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_161167,IEDB_2278476,IEDB_2278477,IEDB_241101,IEDB_558869,IEDB_857743,IEDB_983931,SB_192

NCBI Taxonomy refs (TaxIDs): 5475, 5206, 746128
Reference(s) to other database(s): GTC:G42236TW
Show glycosyltransferases

There is only one chemically distinct structure:

*O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O[C@@H]2[C@@H](O)[C@H](O[C@@H]3[C@@H](O)[C@H](O[C@@H]4[C@@H](O)[C@H](O[C@@H]5[C@@H](O)[C@H](*)O[C@H](CO)[C@H]5O)O[C@H](CO)[C@H]4O)O[C@H](CO[C@@H]4O[C@H](CO[C@@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5O)[C@@H](O)[C@H](O)[C@H]4O)[C@H]3O)O[C@H](CO)[C@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize