Identification and cellular localization of the actin-binding protein ABP-120 from Entamoeba histolytica

Authors: Vargas, Miguel; Sansonetti, Philippe; Guillén, Nancy

Source: Molecular Microbiology, Volume 22, Number 5, December 1996 , pp. 849-857(9)

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Abstract:

Several actin-binding proteins participate in the morphological changes that occur during amoeboid movement. The gene encoding one of these proteins, the gelation factor ABP-120, was identified and characterized from trophozoites of Entamoeba histolytica. The sequence contains 2574 nucleotides, with an open reading frame of 858 amino acids, giving a protein of 93 kDa belonging to the spectrin family. The N-terminal domain of ABP-120 from E. histolytica revealed a consensus site for actin binding homologous to the actin-binding sites of ABP-120 of Dictyostelium discoideum, α-actinin and spectrin. Analysis of the central domain revealed the presence of four repeats of a 73-amino-acid motif constituting 31% of the protein. In addition, a stretch of 105 amino acids was highly divergent when compared with the C-terminal domain of D. discoideum ABP-120. This sequence showed short motifs that are homologous to microtubule-binding domains. We found that ABP-120 from E. histolytica binds to F-actin. In addition, upon motility of the parasite, this protein localized in the pseudopod and the uroid region, implying a role for ABP-120 in movement and capping of surface receptors in E. histolytica.

Document Type: Research article

DOI: http://dx.doi.org/10.1046/j.1365-2958.1996.01535.x

Affiliations: 1: Unité de Pathogénie Microbienne Moléculaire, Institut National de la Santé et de la Recherche Médicale U389, Institut Pasteur, 28 Rue du Dr Roux, 75724 Paris Cédex 15, France.

Publication date: 1996-12-01