A novel saposin-like protein of Entamoeba histolytica with membrane-fusogenic activity

Molecular and Biochemical Parasitology
Julia WinkelmannHeike Bruhn

Abstract

Amoebapores, the pore-forming proteins of Entamoeba histolytica, are major pathogenicity factors of the parasite. Upon a comprehensive survey in the recently completed genome data sets for the protozoon, we identified in addition to the three amoebapore genes, 16 genes which are constitutively expressed and code for structurally similar proteins, all belonging to the family of saposin-like proteins. Here, we recombinantly expressed in bacteria a defined single entity of this expansive amoebic protein family, namely SAPLIP 3. The protein consists of the saposin-like domain only, comparable to amoebapores, and we characterized its interactions with membranes using different assays. In contrast to amoebapores, SAPLIP 3 neither forms pores in liposomes nor permeabilizes bacterial membranes. However, SAPLIP 3 induces leaky fusion of lipid vesicles as evidenced by fluorescence microscopic analysis and by using a fusion assay that monitors the dequenching of a lipophilic dye. The membrane-fusogenic activity of SAPLIP 3 which is dependent on the presence of negatively charged lipids and on acidic pH resembles in combination with the negative surface charge of the protein characteristics of human saposin C. Beside its function as a cofa...Continue Reading

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Citations

Mar 28, 2009·The Journal of Biological Chemistry·John M HarringtonStephen L Hajduk
Apr 9, 2010·Clinical Microbiology Reviews·Alicia HidronAnis Rassi
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Apr 6, 2021·Frontiers in Cellular and Infection Microbiology·Constantin KönigIris Bruchhaus

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