Characterization of a cDNA encoding a cysteine-rich cell surface protein located in the flagellar pocket of the protozoan Trypanosoma brucei.
Characterization of a cDNA encoding a cysteine-rich cell surface protein located in the flagellar pocket of the protozoan Trypanosoma brucei.
复制标题
编码位于原生动物布氏锥虫鞭毛袋中富含半胱氨酸的细胞表面蛋白的 cDNA 的表征。
DOI：
10.1128/mcb.10.9.4506-4517.1990
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发表时间：
1990
影响因子：
5.3
通讯作者：
VanderPloeg,LH
中科院分区：
文献类型：
--
作者：
Lee,MG;Bihain,BE;Russell,DG;Deckelbaum,RJ;VanderPloeg,LH
我们对寄生原生动物布氏锥虫和马马锥虫的编码富含半胱氨酸的酸性整合膜蛋白（CRAM）的 cDNA 进行了表征。与锥虫的其他膜蛋白不同。布鲁氏菌分布在整个细胞表面，CRAM 集中在鞭毛袋中，鞭毛袋是锥虫细胞表面的内陷，内吞作用已被记录在案。因此，CRAM 也定位到位于口袋下方的囊泡，提供其内化的证据。 CRAM 的预计分子量为 130 千道尔顿，并具有信号肽、跨膜结构域和 41 个氨基酸的细胞质延伸。 CRAM 的一个特征是具有大约 66 倍酸性、富含半胱氨酸的 12 个氨基酸重复序列的大型细胞外结构域。 CRAM在包括克氏锥虫在内的不同原生动物物种中是保守的，并且CRAM与真核细胞表面受体具有结构相似性。 CRAM 最显着的同源性是与人类低密度脂蛋白受体的同源性。我们提出 CRAM 作为不同锥虫物种的细胞表面受体。
We have characterized a cDNA encoding a cysteine-rich, acidic integral membrane protein (CRAM) of the parasitic protozoaTrypanosoma bruceiandTrypanosoma equiperdum.Unlike other membrane proteins ofT. brucei,which are distributed throughout the cell surface, CRAM is concentrated in the flagellar pocket, an invagination of the cell surface of the trypanosome where endocytosis has been documented. Accordingly, CRAM also locates to vesicles located underneath the pocket, providing evidence of its internalization. CRAM has a predicted molecular mass of 130 kilodaltons and has a signal peptide, a transmembrane domain, and a 41-amino-acid cytoplasmic extension. A characteristic feature of CRAM is a large extracellular domain with a roughly 66-fold acidic, cysteine-rich 12-amino-acid repeat. CRAM is conserved among different protozoan species, includingTrypanosoma cruzi,and CRAM has structural similarities with eucaryotic cell surface receptors. The most striking homology of CRAM is to the human low-density-lipoprotein receptor. We propose that CRAM functions as a cell surface receptor of different trypanosome species.