Functional characterization of EhADH112: An Entamoeba histolytica Bro1 domain-containing protein
- 作者：Ba脙脙uelos ; C. ; Garc脙脙a-Rivera ; G. ; L脙脙pez-Reyes ; I. ; Orozco ; E.
- 关键词：EhADH112 ; EhCPADH ; Alix/AIP1 ; Bro1 domain ; Adhesin ; Phagocytosis
- 刊名：Experimental Parasitology
- 出版年：2005
- 期刊代码：99_00144894
- 类别：imm
- 出版时间：July, 2005
- 卷：110
- 期：3
- 页码：292-297
- 文件大小：702 K
摘要
EhADH112 is part of the EhCPADH complex, a protein involved in key events of the Entamoeba histolytica host invasion. EhADH112 participates in trophozoite adherence to target cells and in phagocytosis. We report here the finding of two EhADH112 homologues in the E. histolytica genome (EhADH112-like proteins). EhADH112 and its relatives have a Bro1 domain at their amino-terminus and a consensus context for phosphorylation by Src-tyrosine kinases, both involved in signal transduction processes in other organisms. Our findings associate EhADH112 to supplementary functions related to those reported for the Alix/AIP1 family. To elucidate the precise function of EhADH112, we studied the phenotypes displayed by trophozoites transfected with the Ehadh112 full gene. Transfected trophozoites overexpressed a 78 kDa protein, which was mainly targeted to the EhCPADH complex. Moreover, these trophozoites exhibited enhanced phagocytic rates, providing further evidence of EhADH112 contribution to adhesion and phagocytosis activities.