4.4 Article

Structure elucidation and immunological function analysis of a novel β-glucan from the fruit bodies of Polyporus umbellatus (Pers.) Fries

期刊

GLYCOBIOLOGY
卷 22, 期 12, 页码 1673-1683

出版社

OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cws099

关键词

beta-glucan; immunostimulation; lymphocyte; macrophage; structure

资金

  1. PCSIRT [IRT1075]
  2. National Foundation of Natural Science of China [30890142/31070781/81102253]
  3. National Key Basic Research Programs [2010CB529102]
  4. Research Fund for the Doctoral Program of Higher Education [20100001120042]
  5. Priority Academic Program Development of Jiangsu Province Higher Education Institutions

向作者/读者索取更多资源

beta-Glucans derived from various sources such as yeast cell walls and medicinal mushrooms are considered as valuable biological response modifiers for their ability to enhance the activity of immune cells, aid in wound healing and help prevent infections. We herein characterize the structure of a novel water-soluble polysaccharide (Zhuling polysaccharide, ZPS) from the fruit bodies of medicinal mushroom Polyporus umbellatus and investigate its immunobiological function. ZPS has a molecular mass of 2.27 x 10(3) kDa and contains > 90% d-glucose as its monosaccharide constituent. On the basis of partial acid hydrolysis, methylation analysis, Fourier transform infrared spectroscopy and nuclear magnetic resonance spectroscopy and the ideal repeating unit of ZPS is established: (1 -> 6, 1 -> 4)-linked beta-d-glucopyranosyl backbone, substituted at O-3 position of (1 -> 6)-linked beta-d-glucopyranosyl by (1 -> 3)-linked beta-d-glucopyranosyl branches. ZPS consists of approximately 2930 repeating units, each contains a side chain of no more than three residues in length. Functionally, ZPS is a potent activator of B cells, macrophages and dendritic cells. Depletion of ZPS branches causes a substantial reduction in its ability not only to activate B cells in vitro but also to elicit specific IgM production in vivo. Virtually all healthy human subjects possess high-titer circulating antibodies against ZPS backbone, suggesting that ZPS epitope is shared by environmental antigens capable of eliciting adaptive humoral responses in the population.

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