The Biochemical and Functional Characterization of M28 Aminopeptidase Protein Secreted by Acanthamoeba spp. on Host Cell Interaction.

Acanthamoeba are a free-living protozoan whose pathogenic strain can cause severe human diseases, such as granulomatous encephalitis and keratitis. As such, the pathogenic mechanism between humans and Acanthamoeba is still unknown. In our previous study, we identified the secreted Acanthamoeba M28 aminopeptidase (M28AP) and then suggested that M28AP can degrade human C3b and iC3b for inhibiting the destruction of Acanthamoeba spp. with the human immune response. We constructed the produced the recombinant M28AP from a CHO cell, which is a mammalian expression system, to characterize the biochemical properties of Acanthamoeba M28AP. The recombinant M28AP more rapidly hydrolyzed Leu-AMC than Arg-AMC and could be inhibited by EDTA treatment. We show that recombinant M28AP can be delivered into the individual cell line and cause cell line apoptosis in a co-culture model. In conclusion, we successfully investigated the potential molecular characteristics of M28AP.