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

Meseret T. Haile, Anurag Shukla, James Zhen, Michael W. Mather, Suyash Bhatnagar, Joanne M. Morrisey, Zhening Zhang, Akhil B. Vaidya () and Chi-Min Ho ()
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Meseret T. Haile: Columbia University Irving Medical Center
Anurag Shukla: Drexel University College of Medicine
James Zhen: Columbia University Irving Medical Center
Michael W. Mather: Drexel University College of Medicine
Suyash Bhatnagar: Drexel University College of Medicine
Joanne M. Morrisey: Drexel University College of Medicine
Zhening Zhang: Columbia University Irving Medical Center
Akhil B. Vaidya: Drexel University College of Medicine
Chi-Min Ho: Columbia University Irving Medical Center

Nature Communications, 2025, vol. 16, issue 1, 1-9

Abstract: Abstract 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.

Date: 2025
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DOI: 10.1038/s41467-025-64815-y

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