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Plasmodium knowlesi Heat Shock Protein 90s: In Silico Analysis Reveals Unique Druggable Structural Features
Michael O Daniyan1, Harpreet Singh2, Gregory L Blatch3,4
1Department of Pharmacology, Faculty of Pharmacy, Obafemi Awolowo University, Ile-Ife 220005, Nigeria.
International Journal of Molecular Sciences
|December 30, 2025
Summary
Researchers identified the structure and function of Plasmodium knowlesi heat shock proteins 90 (PkHsp90s), revealing a unique drug target. This discovery offers a promising new avenue for developing antimalarial drugs against zoonotic malaria.
Area of Science:
- Malariology
- Parasitology
- Structural Biology
- Drug Discovery
Background:
- Zoonotic malaria, particularly from Plasmodium knowlesi, poses a growing global health threat.
- The urgent need for novel antimalarial pharmacotherapies necessitates exploring new drug targets.
Purpose of the Study:
- To determine the structure, function, and druggability of Plasmodium knowlesi heat shock protein 90s (PkHsp90s).
- To identify potential drug candidates targeting PkHsp90s for antimalarial drug development.
Main Methods:
- Protein sequence and structural analyses
- Phylogenetics
- Protein network mapping
- Protein-ligand interaction studies
- Small molecule docking
- Virtual screening of the ZINC database
Main Results:
- Identified four PkHsp90 isoforms with distinct structural features compared to human Hsp90s.
- Elucidated a plasmodial-specific hydrophobic extension in the GHL motif of cytosolic PkHsp90.
- Discovered novel compounds (ZINC22007970, ZINC724661072, ZINC724661078) that strongly bind to PkHsp90 but not human HSPC1.
Conclusions:
- PkHsp90s represent a druggable target for developing new antimalarial therapies.
- This study provides a molecular framework for rational drug design against zoonotic malaria.
