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<p>The <i>Plasmodium falciparum</i> sodium efflux pump <i>Pf</i>ATP4 is a leading antimalarial target, but suffers from a lack of high-resolution structural information needed to identify functionally important features in conserved regions and guide rational design of next generation inhibitors. Here, we determine a 3.7 Å cryoEM structure of <i>Pf</i>ATP4 purified from CRISPR-engineered <i>P. falciparum</i> parasites, revealing a previously unknown, apicomplexan-specific binding partner, <i>Pf</i>ABP, which forms a conserved, likely modulatory interaction with <i>Pf</i>ATP4. The discovery of <i>Pf</i>ABP presents an unexplored avenue for designing <i>Pf</i>ATP4 inhibitors.</p>

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Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年10月20日

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  • Meseret T. Haile,
  • Anurag Shukla,
  • James Zhen,
  • Michael W. Mather,
  • Suyash Bhatnagar,
  • Joanne M. Morrisey,
  • Zhening Zhang,
  • Akhil B. Vaidya,
  • Chi-Min Ho

摘要

The Plasmodium falciparum sodium efflux pump PfATP4 is a leading antimalarial target, but suffers from a lack of high-resolution structural information needed to identify functionally important features in conserved regions and guide rational design of next generation inhibitors. Here, we determine a 3.7 Å cryoEM structure of PfATP4 purified from CRISPR-engineered P. falciparum parasites, revealing a previously unknown, apicomplexan-specific binding partner, PfABP, which forms a conserved, likely modulatory interaction with PfATP4. The discovery of PfABP presents an unexplored avenue for designing PfATP4 inhibitors.