9XDB
Structure of Plasmodium vivax Perforin-like protein2 pore in acr form
This is a non-PDB format compatible entry.
Summary for 9XDB
| Entry DOI | 10.2210/pdb9xdb/pdb |
| EMDB information | 66761 |
| Descriptor | MAC/Perforin domain containing protein (1 entity in total) |
| Functional Keywords | plasmodium; perforin-like protein; pvplp2, toxin |
| Biological source | Plasmodium vivax (malaria parasite P. vivax) |
| Total number of polymer chains | 3 |
| Total formula weight | 379981.76 |
| Authors | Zhang, Y.,Zhong, L.J.,Song, Y.,Gilbert, R.J.C.,Ni, T.,Yu, X.L. (deposition date: 2025-10-27, release date: 2026-08-12, Last modification date: 2026-09-16) |
| Primary citation | Zhang, Y.,Zhong, L.,Song, Y.,Guo, M.,Ren, K.,Yang, T.,Huang, Y.,Sirotkin, I.,Yi, G.,Jiao, F.,Zhang, P.,Gilbert, R.J.C.,Ni, T.,Yu, X. Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: Malaria-causing Plasmodium parasites must pass through several host cell types to complete their life cycle. This cell traversal is facilitated by perforin-like proteins (PLPs), among which PLP2 is essential for erythrocyte rupture by gametocytes. However, the mechanism by which PLP2 forms pores is not yet understood. Here, we combine cryo-electron microscopy and tomography to reveal the structural basis of Plasmodium vivax PLP2-mediated membrane attack. PvPLP2 assembles on lipid bilayers into heterogeneous arc- and ring-shaped pores with variable stoichiometries. Among them, we determine the structure of a 17-subunit pore complex in which the pore-forming MACPF domains form the central β-barrel, while the peripheral Apicomplexan PLP C-terminal β-pleated sheet (APCβ) domains anchor the complex to the membrane surface. A disulfide-stabilized mutant captures an intermediate pre-pore complex prior to membrane insertion, delineating the structural transitions that underpin β-barrel deployment. Functionally, PvPLP2 acts preferentially on the inner leaflet of the erythrocyte membrane, a specificity driven by its affinity for negatively charged lipids. Together, these findings establish the pore-formation pathway for a key Plasmodium virulence factor and provide a structural framework for rational design of transmission-blocking agents that prevent gametocyte egress. PubMed: 42675073DOI: 10.1038/s41467-026-76236-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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