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TitleStructure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJun 15, 2025
AuthorsEzra T Bekkering / Randy Yoo / Sophia Hailemariam / Fabian Heide / Danton Ivanochko / Matthew Jackman / Nicholas I Proellochs / Rianne Stoter / Geert-Jan van Gemert / Ayana Maeda / Takaaki Yuguchi / Oscar T Wanders / Renate C van Daalen / Maartje R Inklaar / Carolina M Andrade / Pascal W T C Jansen / Michiel Vermeulen / Teun Bousema / Eizo Takashima / John L Rubinstein / Taco W A Kooij / Matthijs M Jore / Jean-Philippe Julien /
PubMed AbstractThe Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet little is known about its molecular assembly. Here, we used cryogenic electron microscopy ...The Pfs230:Pfs48/45 complex forms the basis for leading malaria transmission-blocking vaccine candidates, yet little is known about its molecular assembly. Here, we used cryogenic electron microscopy to elucidate the structure of the endogenous Pfs230:Pfs48/45 complex bound to six potent transmission-blocking antibodies. Pfs230 consists of multiple domain clusters rigidified by interactions mediated through insertion domains. Membrane-anchored Pfs48/45 forms a disc-like structure and interacts with a short C-terminal peptide on Pfs230 that is critical for Pfs230 membrane-retention . Interestingly, membrane retention through this interaction is not essential for transmission to mosquitoes, suggesting that complex disruption is not a mode of action for transmission-blocking antibodies. Analyses of Pfs48/45- and Pfs230-targeted antibodies identify conserved epitopes on the Pfs230:Pfs48/45 complex and provides a structural paradigm for complement-dependent activity of Pfs230-targeting antibodies. Altogether, the antibody-bound Pfs230:Pfs48/45 structure presented improves our molecular understanding of this biological complex, informing the development of next-generation transmission-blocking interventions.
External linksbioRxiv / PubMed:39990443 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 4.7 Å
Structure data

48921

9n5h

EMDB-48921, PDB-9n5h:
Endogenous Pfs230D1-6 in complex with RUPA-97, LMIV230-01, and 2A2 Fab domains
Method: EM (single particle) / Resolution: 3.6 Å

48924

9n5k

EMDB-48924, PDB-9n5k:
Endogenous Pfs230D9-14 in complex with Pfs48/45
Method: EM (single particle) / Resolution: 4.7 Å

48941

9n5o

EMDB-48941, PDB-9n5o:
Endogenous Pfs230D7-8 in complex with 18F25
Method: EM (single particle) / Resolution: 4.32 Å

Source
  • plasmodium falciparum 3d7 (eukaryote)
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / 6-Cys / antibody / CELL ADHESION

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