NCBI PubMed ID:16406275 Publication DOI:10.1016/j.carres.2005.11.036 Journal NLM ID:0043535 Publisher: Elsevier Correspondence: David S. Stephens <dstep01emory.edu> Institutions: Laboratories of Microbial Pathogenesis, VA Medical Center and Division of Infectious Diseases, Atlanta, GA, USA, Departments of Medicine, Emory University School of Medicine, Atlanta, GA, USA
High resolution-magic angle spinning (HRMAS) NMR spectroscopy was applied to serogroup A Neisseria meningitidis (NMA) to determine precise structures of capsular polysaccharide (CPS) expressed on the meningococcal surface. Both the O-acetylated (OAc) NMA parent and a mynC::aphA3 OAc- mutant demonstrated characteristic CPS-derived NMR signals indicating cell-surface expression of CPS, but only the parent expressed O-3 and O-4 acetylation signals. A capsule-defective strain showed no NMR signals for CPS. The (1)H NMR HRMAS spectral patterns correlated with the purified CPS (1)H NMR profiles. HRMAS NMR can distinguish detailed complex carbohydrate structures expressed on bacteria. NMA express both O-3 and O-4 acetylated polymers but not in equimolar ratio amounts in vivo.
NCBI PubMed ID:16406275 Publication DOI:10.1016/j.carres.2005.11.036 Journal NLM ID:0043535 Publisher: Elsevier Correspondence: David S. Stephens <dstep01emory.edu> Institutions: Laboratories of Microbial Pathogenesis, VA Medical Center and Division of Infectious Diseases, Atlanta, GA, USA, Departments of Medicine, Emory University School of Medicine, Atlanta, GA, USA
High resolution-magic angle spinning (HRMAS) NMR spectroscopy was applied to serogroup A Neisseria meningitidis (NMA) to determine precise structures of capsular polysaccharide (CPS) expressed on the meningococcal surface. Both the O-acetylated (OAc) NMA parent and a mynC::aphA3 OAc- mutant demonstrated characteristic CPS-derived NMR signals indicating cell-surface expression of CPS, but only the parent expressed O-3 and O-4 acetylation signals. A capsule-defective strain showed no NMR signals for CPS. The (1)H NMR HRMAS spectral patterns correlated with the purified CPS (1)H NMR profiles. HRMAS NMR can distinguish detailed complex carbohydrate structures expressed on bacteria. NMA express both O-3 and O-4 acetylated polymers but not in equimolar ratio amounts in vivo.
Shibata N, Saitoh T, Tadokoro Y, Okawa Y The cell wall galactomannan antigen from Malassezia furfur and Malassezia pachydermatis contains beta-1,6-linked linear galactofuranosyl residues and its detection has diagnostic potential Microbiology (2009)
3420-3429
The structure was elucidated in this paper NCBI PubMed ID:19389777 Publication DOI:10.1099/mic.0.029967-0 Journal NLM ID:0376646 Publisher: Washington, DC: Kluwer Academic/Plenum Publishers Correspondence: nshibatatohoku-pharm.ac.jp Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, Aoba-ku, Sendai, Japan
Lipophilic yeasts of the genus Malassezia are associated with several skin diseases, such as pityriasis versicolor, Malassezia folliculitis, seborrhoeic dermatitis and atopic dermatitis, and are also increasingly associated with catheter-related fungaemia. The cell wall components of pathogenic micro-organisms behave as an antigen and/or ligand of the innate immune response. Live cells of Malassezia furfur and Malassezia pachydermatis did not react with an anti-α-1,2-mannoside antibody. However, they showed a strong hydrophobicity and reactivity with an anti-β-1,3-glucan antibody compared to those of C. albicans. The cell wall polysaccharides of M. furfur and M. pachydermatis were isolated and their structures analysed by (1)H and (13)C NMR experiments. Both polysaccharides were shown to be β-1,6-linked linear galactofuranosyl polymers with a small amount of mannan. The presence of galactomannan on cells of Malassezia species has not been described previously. The galactomannan did not react with an anti-Aspergillus fumigatus monoclonal antibody which has specificity for β-1,5-linked galactofuranosyl residues. An anti-M. furfur antibody strongly reacted with the galactomannans of M. furfur and M. pachydermatis, but did not react with the galactomannans of Trichophyton rubrum, A. fumigatus or Fonsecaea pedrosoi. The characteristics of the anti-M. furfur antibody suggest that there is potential for diagnosis of Malassezia infections by antigen detection.
Methods: 13C NMR, 1H NMR, NMR-2D, partial acid hydrolysis, ELISA, composition analysis, GPC, ion-exchange chromatography, cell surface hydrophobicity, immunization, flow cytometry analysis Comments, role: Malassezia furfur NBRC 0656 (=CBS 1878), Malassezia pachydermatis NBRC 10064 (=CBS 1879). One of the possible structures; in which a core mannan has a comb-like structure (with multiple -6)aDManp(1- residues); attachment of Galf side chain to one of mannose residues is undetermined
Masuoka J, Hazen KC Cell wall mannan and cell surface hydrophobicity in Candida albicans serotype A and B strains Infection and Immunity72(11) (2004)
6230-6236
NCBI PubMed ID:15501748 Publication DOI:10.1128/IAI.72.11.6230-6236.2004 Journal NLM ID:0246127 Publisher: American Society for Microbiology Correspondence: Masuoka J <jm2nvirginia.edu> Institutions: Department of Pathology, University of Virginia Health System, Charlottesville, USA, Department of Microbiology, University of Virginia Health System, Charlottesville, USA
Cell surface hydrophobicity contributes to the pathogenesis of the opportunistic fungal pathogen Candida albicans. Previous work demonstrated a correlation between hydrophobicity status and changes in the acid-labile, phosphodiester-linked β-1,2-oligomannoside components of the N-linked glycans of cell wall mannoprotein. Glycan composition also defines the two major serotypes, A and B, of C. albicans strains. Here, we show that the cell surface hydrophobicity of the two serotypes is qualitatively different, suggesting that the serotypes may differ in how they modulate cell surface hydrophobicity status. The cell wall mannoproteins from hydrophilic and hydrophobic cells of both serotypes were compared to determine whether the glycan differences due to serotype affect the glycan differences due to hydrophobicity status. Composition analysis showed that the protein, hexose, and phosphate contents of the mannoprotein fraction did not differ significantly among the strains tested. Electrophoretic profiles of the acid-labile mannan differed only with hydrophobicity status, not serotype, though some strain-specific differences were observed. Furthermore, a newly available β-1,2-oligomannoside ladder allowed unambiguous identification of acid-labile mannan components. Finally, to assess whether the acid-stable mannan also affects cell surface hydrophobicity status, this fraction was fragmented into its component branches by acetolysis. The electrophoretic profiles of the acid-stable branches were very similar regardless of hydrophobicity status. However, differences were observed between serotypes. These results support and extend our current model that modification of the acid-labile β-1,2-oligomannoside chain length but not modification of the acid-stable region is one common mechanism by which switching of cell surface hydrophobicity status of C. albicans strains occurs
report error
Found 4 records.
Displayed records from 1 to 4
]
emory.edu>