Identification of a family of BspA like surface proteins of Entamoeba histolytica with novel leucine rich repeats
Identification of a family of BspA like surface proteins of Entamoeba histolytica with novel leucine rich repeats
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DOI：
10.1016/j.molbiopara.2005.08.017
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发表时间：
2006-01-01
影响因子：
1.5
通讯作者：
Stanley, SL
中科院分区：
文献类型：
--
作者：
Davis, PH;Zhang, Z;Stanley, SL
富含亮氨酸的重复序列是细菌和真核生物表面蛋白的识别基序。福赛氏拟杆菌的BSPA蛋白介导细菌与纤维连接蛋白的结合，并含有梅毒螺旋体(TpLRRP)家族的富含亮氨酸的重复序列。在这里，我们发现原虫寄生虫溶组织内阿米巴含有多个BSPA样蛋白，包括一个表面蛋白家族，它具有两个保守的半胱氨酸残基，具有不同于标准的梅毒螺旋体样富亮氨酸重复序列(TpLRRP)的新形式的富亮氨酸重复序列。
Leucine rich repeats serve as recognition motifs for surface proteins from bacteria and eukaryotes. The BspA protein from Bacteroides forsythus mediates bacterial binding to fibronectin and contains leucine rich repeats of the Treponema pallidum (TpLRRP) family. Here we show that the protozoan parasite Entamoeba histolytica contains multiple BspA-like proteins, including a family of surface proteins which possess a new form of a leucine rich repeat that differs from the standard Treponema pallidum- like leucine rich repeat (TpLRRP) by possessing two conserved cysteine residues.