Luján H D, Mowatt M R, Conrad J T, Bowers B, Nash T E
Laboratory of Parasitic Diseases, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA.
J Biol Chem. 1995 Dec 8;270(49):29307-13. doi: 10.1074/jbc.270.49.29307.
Giardia lamblia trophozoites, like most intestinal parasitic protozoa, undergo fundamental biological changes to survive outside the intestine of their mammalian host by differentiating into infective cysts. This complex process entails the coordinated production, processing, and transport of cyst wall constituents for assembly into a protective cyst wall. Yet, little is known about this process and the identity of cyst wall constituents. We previously identified a 26-kDa cyst wall protein, CWP1. In the present work, using monoclonal antibodies to cyst wall antigens, we cloned the gene that encodes a novel 39-kDa cyst wall protein, CWP2. Expression of CWP1 and CWP2 was induced during encystation with identical kinetics. Soon after synthesis, these two proteins combine to form a stable complex, which is concentrated within the encystation-specific secretory granules before incorporation into the cyst wall. Both proteins contain five tandem copies of a 24-residue leucine-rich repeat, a motif implicated in protein-protein interactions. Unlike CWP1, CWP2 has an extremely basic 121-residue COOH-terminal extension that might be involved in the sorting of these proteins to the secretory granules.
与大多数肠道寄生原生动物一样,蓝氏贾第鞭毛虫滋养体通过分化形成感染性包囊,从而发生根本性的生物学变化,以便在其哺乳动物宿主的肠道外生存。这个复杂的过程需要协调生产、加工和运输包囊壁成分,以组装成保护性包囊壁。然而,对于这个过程以及包囊壁成分的身份知之甚少。我们之前鉴定出一种26 kDa的包囊壁蛋白CWP1。在目前的工作中,我们使用针对包囊壁抗原的单克隆抗体,克隆了编码一种新型39 kDa包囊壁蛋白CWP2的基因。在包囊化过程中,CWP1和CWP2的表达以相同的动力学被诱导。合成后不久,这两种蛋白结合形成一个稳定的复合物,该复合物在被整合到包囊壁之前,集中在包囊化特异性分泌颗粒内。这两种蛋白都含有五个串联重复的24个残基的富含亮氨酸重复序列,这是一个与蛋白质-蛋白质相互作用有关的基序。与CWP1不同,CWP2有一个由121个残基组成的极其碱性的COOH末端延伸,可能参与这些蛋白向分泌颗粒的分选。