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首页> 外文期刊>Infection and immunity >Analysis of mannoproteins from blastoconidia and hyphae of Candida albicans with a common epitope recognized by anti-complement receptor type 2 antibodies.
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Analysis of mannoproteins from blastoconidia and hyphae of Candida albicans with a common epitope recognized by anti-complement receptor type 2 antibodies.

机译：分析来自白色念珠菌的白色种念珠菌和菌丝中的甘露糖蛋白，具有被2型抗补体受体抗体识别的常见表位。

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摘要

Mannoproteins of approximately 50 kDa from blastoconidia and 60 kDa from hyphae of Candida albicans reacted in Western blots (immunoblots) with either a polyclonal rabbit antiserum (CA-7) or a monoclonal antibody (CA-A) to the C. albicans C3d-binding protein (complement receptor type 2). The glycosylated nature of these proteins was demonstrated by their reactivity with concanavalin A and by selective labeling with the biotin-hydrazide reagent following periodate oxidation. Differences in the oligosaccharides of these proteins were observed in regard to their reactivity with lectin-peroxidase reagents and sensitivity to glycosidases such as N-glycanase or endoglycosidase F (but not endoglycosidase H). The 60-kDa mannoprotein reacted with wheat germ agglutinin, while the 50-kDa mannoprotein did not. Treatment of the 60-kDa mannoprotein with the glycosidases mentioned above resulted in its conversion into a species of 40 to 45 kDa. Enzyme treatment had no obvious effect on the electrophoretic mobility of the 50-kDa species from blastoconidia. Both the 50- and 60-kDa glycoproteins remained immunoreactive after treatment with the glycosidases. Reactivities of the two mannoproteins to neuraminidase also differed. Finally, the 50-kDa (blastoconidia) and the 60-kDa (hyphae) mannoproteins were purified by using ion-exchange chromatography and electroelution. The purified proteins differed in net charge, the 60-kDa species having a more acidic pI. Functional activity of the purified mannoproteins was demonstrated, as each inhibited the rosetting of antibody-sensitized sheep erythrocytes conjugated with iC3b or C3d by hyphae. Thus, an epitope(s) common to both a mycelial and blastoconidial mannoprotein is associated with a structurally different oligosaccharide for each growth form.
机译：来自稻瘟病菌的约50 kDa的甘露糖蛋白和来自白色念珠菌的菌丝的60 kDa的甘露蛋白在Western印迹（免疫印迹）中与多克隆兔抗血清（CA-7）或白色念珠菌C3d结合的单克隆抗体（CA-A）反应蛋白（2型补体受体）。这些蛋白质的糖基化性质通过其与伴刀豆球蛋白A的反应性以及通过高碘酸氧化后用生物素酰肼试剂的选择性标记来证明。观察到这些蛋白的寡糖与凝集素过氧化物酶试剂的反应性以及对糖苷酶（如N-糖基酶或内切糖苷酶F（但未见内切糖苷酶H））的敏感性方面存在差异。 60 kDa的甘露糖蛋白与小麦胚芽凝集素反应，而50 kDa的甘露糖蛋白则没有。用上述糖苷酶处理60-kDa甘露糖蛋白导致其转化为40-45kDa的物种。酶处理对稻瘟病菌50 kDa物种的电泳迁移率没有明显影响。用糖苷酶处理后，50kDa和60kDa的糖蛋白均保持免疫反应。两种甘露糖蛋白对神经氨酸酶的反应性也不同。最后，通过离子交换色谱和电洗脱纯化50 kDa（胚芽孢杆菌）和60 kDa（菌丝）甘露糖蛋白。纯化的蛋白质的净电荷有所不同，60 kDa的蛋白质具有更高的酸性pI。证实了纯化的甘露糖蛋白的功能活性，因为它们均抑制了通过菌丝与iC3b或C3d结合的抗体致敏绵羊红细胞的玫瑰花结。因此，对于每种生长形式，菌丝体和囊胚性甘露糖蛋白共同的一个或多个表位与结构上不同的寡糖相关。

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