Adherence to colonic mucosa is conducive to the continued reproduction of parasites and tissue damage by the products secreted by amoebae, such as the pore-forming peptide amoebapore [66], which permits a massive influx of extracellular Ca+2 that is combined with the release of amoebic proteases at the site of contact, with the subsequent degradation of substrates.
Incubation of amoebae with type-I collagen not only promotes collagenase activity but also increases the secretion of other CPs [15], and together with Ca2+, type-I collagen can induce the activation of several amoebic genes related to virulence factors, such as amoebapore C and EhCP5, along with the stress-induced protein HSP70 and the ribosomal protein L27a [138].
Using silenced strains, the authors reported that this phenomenon occurred independently of the cytolytic amoebapore but required galactose-inhibitable parasite adhesion, likely involving amoebic Gal/GalNAc lectin, and active E.
In thiswork, the authors postulate that amoebae first bind to intestinal epithelial cells and then lyse those cells through the action of amoebapore [175, 176].
histolytica, the only available strategy requires the use of the G3 strain in which the amoebapore is silenced as a genetic background to perform the knockdown of the protease gene.
Mirelman, "Antisense inhibition of amoebapore expression in Entamoeba histolytica causes a decrease in amoebic virulence," Molecular Microbiology, vol.
