Glycoproteins of Pneumocystis carinii: characterization by electrophoresis and microscopy.

Glycoproteins of Pneumocystis carinii: characterization by electrophoresis and microscopy.
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卡氏肺囊虫的糖蛋白:通过电泳和显微镜进行表征。

DOI:
10.1093/infdis/158.6.1353
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发表时间:
1988
期刊:
The Journal of infectious diseases
影响因子:
--
通讯作者:
Shanley,JD
Shanley,JD
中科院分区:
--
文献类型:
--
作者:
Pesanti,EL;Shanley,JD

文献摘要

被引文献

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糖蛋白是细胞表面结构的组成部分,参与病原微生物对宿主细胞的粘附。我们对卡氏肺孢子虫的糖蛋白进行了初步研究,用生物素标记的凝集素与亲和素-过氧化物酶反应,检测卡氏肺孢子虫分离蛋白中的糖蛋白。cariniand对整个生物体时,使用光学显微镜。P. carini与大鼠细胞糖蛋白明显不同。P中存在多种糖蛋白。cariniand对刀豆球蛋白A和麦胚凝集素都表现出强烈的反应性。这些凝集素反应与分离的蛋白质也染色酒精固定P。carinii和细胞外颗粒物质只存在于P。卡里尼制剂。在P. carinii,用胶体金标记的伴刀豆球蛋白A染色,我们发现凝集素结合到生物体的外表面和从外表面发出的管状延伸。
Glycoproteins are integral components of cell-surface structure and participate in adherence of pathogenic microbes to host cells. We have initiated studies of the glycoproteins ofPneumocystis carinii.Biotin-conjugated lectins, followed by reaction with avidin-peroxidase, were used to detect glycoproteins in electrophoretically separated proteins ofP. cariniiand on whole organisms when using light microscopy. Glycoproteins ofP. cariniiwere clearly different from rat cell glycoproteins. Multiple glycoproteins were present inP. cariniiand exhibited intense reactivity to both concanavalin A and wheat-germ agglutinin. Those lectins that reacted with the electrophoretically separated proteins also stained both alcohol-fixedP. cariniiand the extracellular granular material present only inP. cariniipreparations. In electron micrographs ofP. carinii,which were stained with colloidal gold-labeled concanavalin A, we found that the lectin bound to the outer surface of the organisms and to the tubular extensions emanating from the exterior surface.