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© Research
Publication : Molecular microbiology

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 01 Dec 1996

Vargas M, Sansonetti P, Guillén N

Link to Pubmed [PMID] – 8971707

Mol. Microbiol. 1996 Dec;22(5):849-57

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, alpha-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.

http://www.ncbi.nlm.nih.gov/pubmed/8971707