Gallo J M, Schrével J
Eur J Cell Biol. 1985 Mar;36(2):163-8.
A Nonidet P 40 insoluble fraction was isolated from Trypanosoma brucei and was used to raise a monoclonal antibody (5E9). The antigen was localized by indirect immunofluorescence in the flagellum of T. brucei and of two species of euglenoids, Euglena gracilis and Distigma proteus. In immunoblot analysis, 5E9 appeared to bind to paraflagellar rod proteins PFR1 and PFR2 of T. brucei (72000 and 75000 mol. wt.) and of E. gracilis (67000 and 76000 mol. wt.). The presence of a common epitope in paraflagellar rod proteins from species of trypanosomes and euglenoids shows that despite distinct structures of the rods some identical domain exists in the proteins that could be involved in their supramolecular assembly into a similar organelle. The antigenic determinant defined by 5E9 was also shown to be present in a 87000 molecular weight polypeptide located in the proximal part of the flagellum of Crithidia oncopelti in which a paraflagellar rod is not detectable at the ultrastructural level.
从布氏锥虫中分离出一种不溶于诺乃洗涤剂P40的组分，并用其制备单克隆抗体（5E9）。通过间接免疫荧光法将该抗原定位在布氏锥虫以及两种裸藻（纤细裸藻和变形陀螺藻）的鞭毛中。在免疫印迹分析中，5E9似乎与布氏锥虫（分子量分别为72000和75000）以及纤细裸藻（分子量分别为67000和76000）的副鞭毛杆蛋白PFR1和PFR2结合。锥虫和裸藻的副鞭毛杆蛋白中存在共同表位，这表明尽管鞭杆结构不同，但这些蛋白中存在一些相同的结构域，可能参与它们组装成类似细胞器的超分子过程。由5E9定义的抗原决定簇也存在于卡氏住白虫鞭毛近端的一种分子量为87000的多肽中，在该虫超微结构水平上未检测到副鞭毛杆。
