Gigliotti F
Department of Pediatrics University of Rochester School of Medicine, New York 14642.
J Infect Dis. 1992 Feb;165(2):329-36. doi: 10.1093/infdis/165.2.329.
All Pneumocystis carinii, irrespective of their host of origin, express an abundant mannosylated surface glycoprotein. While this molecule is commonly referred to as gp120, some variation in the size of this molecule has been noted. Monoclonal antibodies produced to this molecule from ferret, mouse, rat, and human P. carinii made it possible to distinguish the glycoprotein from P. carinii of each host by immunoblot and indirect immunofluorescence assays. The glycoprotein varied in size (approximately 95-140 kDa) depending on the host and method of preparation. One shared epitope involving the mannose part of the glycoprotein was identified, suggesting that despite size and antigenic differences these are homologous molecules. These results indicate the existence of host species-specific serotypes of P. carinii. Referring to this molecule by its molecular mass may be confusing; therefore, it is suggested that this glycoprotein be called surface glycoprotein A, as this was the initial molecule of P. carinii to be isolated and partially characterized.
所有卡氏肺孢子虫,无论其来源宿主是什么,都会表达一种丰富的甘露糖基化表面糖蛋白。虽然该分子通常被称为gp120,但已注意到该分子大小存在一些差异。用来自雪貂、小鼠、大鼠和人类卡氏肺孢子虫产生的针对该分子的单克隆抗体,通过免疫印迹和间接免疫荧光测定法,能够区分来自每个宿主的卡氏肺孢子虫的糖蛋白。该糖蛋白的大小(约95 - 140 kDa)因宿主和制备方法而异。鉴定出一个涉及该糖蛋白甘露糖部分的共同表位,这表明尽管存在大小和抗原差异,但这些是同源分子。这些结果表明存在卡氏肺孢子虫的宿主物种特异性血清型。按其分子量来称呼该分子可能会造成混淆;因此,建议将这种糖蛋白称为表面糖蛋白A,因为这是最初分离并部分表征的卡氏肺孢子虫分子。