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Hijacking Plasmodium AspRS to halt protein synthesis
A Streptomyces natural product, dealanylascamycin (DACM, yellow), inhibits a key Plasmodium enzyme by mimicking its natural substrate. It hijacks the enzymatic reaction, leading to the formation of a DACM-aspartic acid adduct that occupies the enzyme’s active site, thereby blocking protein synthesis. This novel mechanism represents a promising new strategy for antimalarial therapy. Ketprasit et al. 2025
Image Credit: Nutpakal Ketprasit, Leann Tilley, Stanley C. Xie
Citation: (2025) PLoS Pathogens Issue Image | Vol. 21(7) August 2025. PLoS Pathog 21(7): ev21.i07. https://doi.org/10.1371/image.ppat.v21.i07
Published: August 7, 2025
Copyright: © 2025 . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
A Streptomyces natural product, dealanylascamycin (DACM, yellow), inhibits a key Plasmodium enzyme by mimicking its natural substrate. It hijacks the enzymatic reaction, leading to the formation of a DACM-aspartic acid adduct that occupies the enzyme’s active site, thereby blocking protein synthesis. This novel mechanism represents a promising new strategy for antimalarial therapy. Ketprasit et al. 2025
Image Credit: Nutpakal Ketprasit, Leann Tilley, Stanley C. Xie