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Carbohydrate epitopes in glycoprotein from the opportunistic fungal pathogen Scedosporium apiospermum
Hot aqueous extraction of Scedosporium apiospermum mycelium provided glycoprotein (HET-PR-Sa) containing 37% protein and Rha, Rib, Ara, Man, Gal, Glc, and GlcNH 2 in a 26:14:17:22:10:5:6 molar ratio. HPSEC showed a mixture. HET-PR-Sa, on reductive, alkaline β-elimination at 25 °C, gave nonreducing o...
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Published in: | Carbohydrate polymers 2011-05, Vol.85 (2), p.349-355 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Hot aqueous extraction of
Scedosporium apiospermum mycelium provided glycoprotein (HET-PR-Sa) containing 37% protein and Rha, Rib, Ara, Man, Gal, Glc, and GlcNH
2 in a 26:14:17:22:10:5:6 molar ratio. HPSEC showed a mixture. HET-PR-Sa, on reductive, alkaline β-elimination at 25
°C, gave nonreducing oligosaccharide epitopes (OLIGO-Sa) from
O-linked protein and a polymer (HET-PR-Sa-de-O), which was then β-eliminated at 100
°C to give polysaccharide (HET-Sa). The structure of each fraction (methylation, NMR, and ESI-MS analysis) differed from those of a peptidoglycan (PRM-Pb) from mycelium of related, opportunistic pathogen,
Pseudallescheria boydii. The predominant nonreducing oligosaccharide formed on β-elimination of PRM-Pb was hexasaccharide
3, whereas those (OLIGO-Sa) from HET-PR-Sa were tetra-
2 and mixed pentasaccharides. Trisaccharide
1 was also identified and is a conserved structure in both fungi. Structural differences confirmed that
S.
apiospermum is not an anamorph of a
P. boydii teleomorph. |
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ISSN: | 0144-8617 1879-1344 |
DOI: | 10.1016/j.carbpol.2011.02.033 |