Pinto MR, Gorin PA, Wait R, Mulloy B, Barreto-Bergter E Structures of the O-linked oligosaccharides of a complex glycoconjugate from Pseudallescheria boydii Glycobiology15(10) (2005)
895-904
The structure was elucidated in this paper NCBI PubMed ID:15932920 Publication DOI:10.1093/glycob/cwi084 Journal NLM ID:9104124 Publisher: IRL Press at Oxford University Press Correspondence: eliana.bergtermicro.ufrj.br Institutions: Laboratory for Molecular Structure, National Institute for Biological Standards and Control, South Mimms, UK, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Curitiba, Brazil, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Faculty of Medicine, Kennedy Institute of Rheumatology Division,Imperial College London, London, UK, Faculty of Medicine, Kennedy Institute, Imperial College London, London, UK, Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Hertfordshire, UK
Nonreducing O-linked oligosaccharides were obtained from the peptidorhamnomannan of mycelia of Pseudallescheria boydii by alkaline β-elimination under reducing conditions. They were separated by GPC chromatography to give three oligosaccharide fractions. The major oligosaccharide from fraction 1 was characterized by a combination of techniques including electrospray ionization quadrupole time-of-flight tandem mass spectrometry (ESI MS/MS), matrix-assisted laser desorption ionization mass spectrometry (MALDI MS), nuclear magnetic resonance (NMR), and methylation gas-liquid chromatography-mass spectrometry (GC-MS) analysis. It was branched, with a principal chain of α-Rhap-(1→3)-α-Rhap-(1→3)-α-Manp-(1→2)-Man-ol substituted at O-6 of mannitol with an α-Glcp-(1→4)-β-Galp group. Species containing one and two additional α-Glcp-(1→4) substituents in the rhamnose branch were also present. The major component of fraction 2 was a substructure of oligosaccharide-1, lacking a hexose from the Glc-Gal branch. Fraction 3 contained a mixture of smaller, unbranched, oligosaccharides. In hapten inhibition tests, fractions 1 and 2 blocked the reaction between peptidorhamnomannan (PRM) and rabbit anti-P. boydii mycelium hyperimmune serum by ~75%, whereas fraction 3 inhibited by ~55%.
ESI MS, ELISA, mycelia, ESI MS/MS, MALDI MS, methylation-GC-MS, Pseudallescheria boydii mycelia, methylation GC-MS, Psedallescheria boydii
Pinto MR, Gorin PA, Wait R, Mulloy B, Barreto-Bergter E Structures of the O-linked oligosaccharides of a complex glycoconjugate from Pseudallescheria boydii Glycobiology15(10) (2005)
895-904
The structure was elucidated in this paper NCBI PubMed ID:15932920 Publication DOI:10.1093/glycob/cwi084 Journal NLM ID:9104124 Publisher: IRL Press at Oxford University Press Correspondence: eliana.bergtermicro.ufrj.br Institutions: Laboratory for Molecular Structure, National Institute for Biological Standards and Control, South Mimms, UK, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Curitiba, Brazil, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Faculty of Medicine, Kennedy Institute of Rheumatology Division,Imperial College London, London, UK, Faculty of Medicine, Kennedy Institute, Imperial College London, London, UK, Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Hertfordshire, UK
Nonreducing O-linked oligosaccharides were obtained from the peptidorhamnomannan of mycelia of Pseudallescheria boydii by alkaline β-elimination under reducing conditions. They were separated by GPC chromatography to give three oligosaccharide fractions. The major oligosaccharide from fraction 1 was characterized by a combination of techniques including electrospray ionization quadrupole time-of-flight tandem mass spectrometry (ESI MS/MS), matrix-assisted laser desorption ionization mass spectrometry (MALDI MS), nuclear magnetic resonance (NMR), and methylation gas-liquid chromatography-mass spectrometry (GC-MS) analysis. It was branched, with a principal chain of α-Rhap-(1→3)-α-Rhap-(1→3)-α-Manp-(1→2)-Man-ol substituted at O-6 of mannitol with an α-Glcp-(1→4)-β-Galp group. Species containing one and two additional α-Glcp-(1→4) substituents in the rhamnose branch were also present. The major component of fraction 2 was a substructure of oligosaccharide-1, lacking a hexose from the Glc-Gal branch. Fraction 3 contained a mixture of smaller, unbranched, oligosaccharides. In hapten inhibition tests, fractions 1 and 2 blocked the reaction between peptidorhamnomannan (PRM) and rabbit anti-P. boydii mycelium hyperimmune serum by ~75%, whereas fraction 3 inhibited by ~55%.
ESI MS, ELISA, mycelia, ESI MS/MS, MALDI MS, methylation-GC-MS, Pseudallescheria boydii mycelia, methylation GC-MS, Psedallescheria boydii
Bittencourt VC, Figueiredo RT, da Silva RB, Mourão-Sá DS, Fernandez PL, Sassaki GL, Mulloy B, Bozza MT, Barreto-Bergter E An α-glucan of Pseudallescheria boydii is involved in fungal phagocytosis and toll-like receptor activation Journal of Biological Chemistry281(32) (2006)
22614-22623
The structure was elucidated in this paper NCBI PubMed ID:16766532 Publication DOI:10.1074/jbc.M511417200 Journal NLM ID:2985121R Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology Correspondence: Bozza MT <mbozzamicro.ufrj.br>; Barreto-Bergter E <eliana.bergtermicro.ufrj.br> Institutions: Departamento de Microbiologia Geral, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Departamento de Imunologia, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil, Departamento de Bioquímica, Universidade Federal do Paraná, Parańa, Brazil, National Institute for Biological Standards and Control, Hertfordshire, UK
The host response to fungi is in part dependent on activation of evolutionarily conserved receptors, including toll-like receptors and phagocytic receptors. However, the molecular nature of fungal ligands responsible for this activation is largely unknown. Herein, we describe the isolation and structural characterization of an α-glucan from Pseudallescheria boydii cell wall and evaluate its role in the induction of innate immune response. These analyses indicate that α-glucan of P. boydii is a glycogen-like polysaccharide consisting of linear 4-linked α-D-Glcp residues substituted at position 6 with α-D-Glcp branches. Soluble α-glucan, but not β-glucan, led to a dose-dependent inhibition of conidia phagocytosis. Furthermore, a significant decrease in the phagocytic index occurred when α-glucan from conidial surface was removed by enzymatic treatment with α- amyloglucosidase, thus indicating an essential role of α-glucan in P. boydii internalization by macrophages. α-Glucan stimulates the secretion of inflammatory cytokines by macrophages and dendritic cells; again this effect is abolished by treatment with α-amyloglucosidase. Finally, α-glucan induces cytokine secretion by cells of the innate immune system in a mechanism involving toll-like receptor 2, CD14, and MyD88. These results might have relevance in the context of infections with P. boydii and other fungi, and α-glucan could be a target for intervention during fungal infections.
Methods: 13C NMR, 1H NMR, methylation, GC-MS, ELISA, acid hydrolysis, GC, biological assays, GPC, enzymatic digestion, extraction, acetylation, HPTLC, cytokine production, phenol-sulfuric acid assay, phagocytosis assay, Folin phenol reagent method Biological activity: α-glucan induces TNF release by macrophages through TLR2 and CD14; the secretion of TNF induced by α-glucan was abolished from MyD88-/- macrophages; α-glucan participates in the phagocytosis of conidia and that TLR2 and CD14 are involved in the innate immune activation upon the recognition of α-glucan Comments, role: the structure shown in fig.2 contains a terminal α-D-Glcp residue that contradicts polymeric structure; location of ''C'' mark seems to be erroneous. NMR data assigments were corrected by CSDB stuff (NMR data for residue C were assigned for branched -4,6)aDGlcp(1- residue; NMR data for residue A were assigned to residue marked C in the paper
Related record ID(s): 45019 NCBI Taxonomy refs (TaxIDs):5597 Reference(s) to other database(s): GTC:G65541PQ Show glycosyltransferases
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(later renamed to: Scedosporium boydii)
]; infection due to Pseudallescheria boydii [ICD11: XN6BV 
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