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Publication Abstract from PubMed

Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin family, participates in actin dynamics, and here we report our studies of this protein using both structural and functional approaches. The X-ray crystal structure of EhCoactosin resembles that of human coactosin-like protein, with major differences in the distribution of surface charges and the orientation of terminal regions. According to in vitro binding assays, full-length EhCoactosin binds both F- and G-actin. Instead of acting to depolymerize or severe F-actin, EhCoactosin directly stabilizes the polymer. When EhCoactosin was visualized in E. histolytica cells using either confocal imaging or total internal reflectance microscopy, it was found to colocalize with F-actin at phagocytic cups. Over-expression of this protein stabilized F-actin and inhibited the phagocytic process. EhCoactosin appears to be an unusual type of coactosin involved in E. histolytica actin dynamics.

EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica.,Kumar N, Somlata, Mazumder M, Dutta P, Maiti S, Gourinath S PLoS Pathog. 2014 Sep 11;10(9):e1004362. doi: 10.1371/journal.ppat.1004362., eCollection 2014 Sep. PMID:25210743^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.