ArticleCancers2026
Structure-Function Analysis of Individual Reversion Variants of the Engineered Mpp46Aa1 (PS2Aa1) N65 Protein.
Article in Cancers, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundMpp46Aa1 (formerly PS2Aa1) is a β-pore-forming protein produced by Bacillus thuringiensis that exhibits selective cytotoxicity against cancer cells. Protein engineering has generated variants with improved antitumor activity, including the N65 variant, which contains three amino acid substitutions.
objectiveIn this study, three individual reversion variants of N65 were generated by site-directed mutagenesis to determine the contribution of each substitution to cytotoxicity, selectivity, and cell death mechanisms in the colorectal cancer cell lines SW480 and SW620 and the non-tumorigenic colonic epithelial cell line NCM460.
methodsRecombinant proteins were purified and evaluated using AlamarBlue viability assays, Annexin V/Cy3 staining, caspase-3/7 and caspase-9 activation assays, and JC-1 mitochondrial membrane potential analysis.
resultsThe reversion variants differentially affected the biological activity of N65. Among them, the D34N variant exhibited low IC
conclusionsThese findings demonstrate that the three substitutions present in N65 contribute unequally to its biological activity and identify residue 34 as a key determinant of Mpp46Aa1 cytotoxicity. This study provides structural and functional insights that support the rational engineering of parasporins with enhanced antitumor selectivity.
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