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糖基化对重组新型隐球菌甘露糖蛋白刺激的T细胞反应的贡献。

Contribution of glycosylation to T cell responses stimulated by recombinant Cryptococcus neoformans mannoprotein.

作者信息

Specht Charles A, Nong Shuhua, Dan Jennifer M, Lee Chrono K, Levitz Stuart M

机构信息

University of Massachusetts Medical School, Worcester, MA 01605, USA.

出版信息

J Infect Dis. 2007 Sep 1;196(5):796-800. doi: 10.1086/520536. Epub 2007 Jul 20.

Abstract

Mannoproteins are major antigens driving T cell responses to the opportunistic fungus Cryptococcus neoformans. To investigate the role played by mannosylation, an immunoreactive cryptococcal mannoprotein was expressed recombinantly in E. coli and Pichia pastoris, resulting in unglycosylated and mannosylated proteins, respectively. The Pichia-derived antigen stimulated stronger major histocompatibility class II-restricted T cell responses. Moreover, responses were potently inhibited if the antigen was chemically deglycosylated or if mannose receptors were blocked with mannans. Thus, mannosylation is critical for optimal T cell responses to a fungal antigen and should be taken into account when vaccines to protect against mycoses are designed.

摘要

甘露糖蛋白是驱动T细胞对机会性真菌新型隐球菌产生反应的主要抗原。为了研究甘露糖基化所起的作用,一种具有免疫反应性的隐球菌甘露糖蛋白分别在大肠杆菌和毕赤酵母中重组表达,结果分别产生了未糖基化和甘露糖基化的蛋白。源自毕赤酵母的抗原刺激产生更强的主要组织相容性复合体II类限制性T细胞反应。此外,如果抗原经化学去糖基化处理或用甘露聚糖阻断甘露糖受体,则反应会受到强烈抑制。因此,甘露糖基化对于针对真菌抗原的最佳T细胞反应至关重要,在设计预防真菌病的疫苗时应予以考虑。

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