Bruhn H, Leippe M
Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, D-20359 Hamburg, Germany.
Biochim Biophys Acta. 2001 Sep 3;1514(1):14-20. doi: 10.1016/s0005-2736(01)00345-5.
Amoebapores, the pore-forming proteins of Entamoeba histolytica, have been shown to play a pivotal role in the pathogenicity of the protozoan parasite. They belong to the functionally diverse family of saposin-like proteins (SAPLIPs) characterized by a conserved pattern of cysteine residues and the ability to interact with lipids. Here, we report the identification of genomic sequences encoding presumably novel SAPLIPs in E. histolytica and classify them in the structural and functional context provided by known family members. The genes of altogether 15 SAPLIPs are transcribed in the axenically cultured trophozoites as evidenced by reverse transcriptase-polymerase chain reaction. Interestingly, a remarkable sequence variety with a strong resemblance to that of known, functionally diverse SAPLIPs is present in this archaic, unicellular organism.
溶组织内阿米巴的成孔蛋白阿米巴穿孔素已被证明在这种原生动物寄生虫的致病性中起关键作用。它们属于功能多样的类鞘脂激活蛋白样蛋白（SAPLIPs）家族，其特征是具有保守的半胱氨酸残基模式以及与脂质相互作用的能力。在此，我们报告了在溶组织内阿米巴中鉴定出可能编码新型SAPLIPs的基因组序列，并在已知家族成员提供的结构和功能背景下对它们进行分类。通过逆转录聚合酶链反应证明，在无菌培养的滋养体中总共15种SAPLIPs的基因被转录。有趣的是，在这种古老的单细胞生物中存在着与已知功能多样的SAPLIPs序列极为相似的显著序列多样性。
