Journal article
Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator
Nature communications, v 16(1), 9092
20 Oct 2025
PMID: 41115914
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The
Plasmodium falciparum
sodium efflux pump
Pf
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
Pf
ATP4 purified from CRISPR-engineered
P. falciparum
parasites, revealing a previously unknown, apicomplexan-specific binding partner,
Pf
ABP, which forms a conserved, likely modulatory interaction with
Pf
ATP4. The discovery of
Pf
ABP presents an unexplored avenue for designing
Pf
ATP4 inhibitors.
Here, the authors present the 3.7 Å cryoEM structure of native sodium efflux pump PfATP4 from
Plasmodium falciparum
, revealing a bound protein that they term apicomplexan-specific essential binding partner (PfABP).
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Details
- Title
- Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator
- Creators
- Meseret T. Haile - Columbia University Irving Medical CenterAnurag Shukla - Drexel UniversityJames Zhen - Columbia University Irving Medical CenterMichael W. Mather - Drexel UniversitySuyash Bhatnagar - Drexel UniversityJoanne M. Morrisey - Drexel UniversityZhening Zhang - Columbia University Irving Medical CenterAkhil B. Vaidya (Corresponding Author) - Drexel UniversityChi-Min Ho - Columbia University Irving Medical Center
- Publication Details
- Nature communications, v 16(1), 9092
- Publisher
- Nature Publishing Group
- Number of pages
- 9
- Grant note
- DP5OD029613; R01AI132508; R01AI154499 / U.S. Department of Health & Human Services | National Institutes of Health (NIH) (https://doi.org/10.13039/100000002)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology; [Retired Faculty]
- Web of Science ID
- WOS:001597726000007
- Scopus ID
- 2-s2.0-105019333703
- Other Identifier
- 991022123313504721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology