Characterization of Entamoeba histolytica α-actinin2
2007 (English)In: Molecular and Biochemical Parasitology, Vol. 154, 82-89 p.Article in journal (Refereed) Published
We have cloned and characterized a second α-actinin isoform in Entamoeba histolytica. This protein, α-actinin2, has a N-terminal actin-binding domain, a C-terminal calcium-binding domain and an intervening rod domain containing two spectrin repeats. The protein binds and cross-links actin filaments in a calcium-dependent manner. Therefore α-actinin2 is a genuine α-actinin except for the shorter rod domain compared to the rod domain of isoforms of higher organisms.
A α-actinin-like protein has previous been implicated in the adherence to the host cell and infection. It is therefore possible that α-actinin2 is involved in mechanism of infection, and in particular in reorganisation of the parasite's cytoskeleton that follows on adherence.
E. histolytica α-actinin2 represents one of the first members of the spectrin superfamily where well defined spectrin repeats are found. The isolation and characterization of this second α-actinin isoform is valuable not only into the study of E. histolytica infection mechanisms, but also for understanding the evolution processes of the spectrin superfamily.
Place, publisher, year, edition, pages
2007. Vol. 154, 82-89 p.
α-Actinin, Entamoeba histolytica, Actin
IdentifiersURN: urn:nbn:se:umu:diva-16098DOI: 10.1016/j.molbiopara.2007.04.010OAI: oai:DiVA.org:umu-16098DiVA: diva2:155771