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Cited by 17Malaria Research and ControlAdvanced Electron Microscopy Techniques and ApplicationsBird parasitology and diseases

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Cryo-EM structure of endogenous Plasmodium falciparum Pfs230 and Pfs48/45 fertilization complex

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Dietrich, Melanie H., Chmielewski, Jill, Chan, Li-Jin, Tan, Li Lynn, Adair, Amy, Lyons, Frankie M. T., Gabriela, Mikha, Lopaticki, Sash, Dite, Toby A., Dagley, Laura F., Pazzagli, Lucia, Gupta, Priya, Kamil, Mohd, Vaughan, Ashley M., Rojrung, Rattanaporn, Abraham, Anju, Mazhari, Ramin, Longley, Rhea J., Zeglinski, Kathleen, Gouil, Quentin, Mueller, Ivo, Fabb, Stewart A., Shandre-Mugan, Rekha, Pouton, Colin W., Glukhova, Alisa, Shakeel, Shabih, Tham, Wai-Hong·2025·Science
DOI 10.1126/science.ady0241

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Abstract

Malaria parasite fertilization occurs in the midgut of a female Anopheles mosquito. Blocking fertilization within the mosquito can prevent malaria transmission. Plasmodium falciparum Pfs230 and Pfs48/45 proteins are critical for male fertility and transmission of the malaria parasite. They form a core fertilization complex, but it is unknown how they interact. We determined a cryo–electron microscopy structure of the endogenous Pfs230-Pfs48/45 complex showing that Pfs48/45 interacts with Pfs230 domains 13 and 14. Transgenic parasite lines with these domains removed were defective in Pfs230 gamete localization and showed reduced oocyst formation. Nanobodies against domains 13 and 14 inhibited Pfs230-Pfs48/45 complex formation and reduced transmission, and structural analyses revealed their epitopes. These Pfs230 domains were targets of naturally acquired immunity and immune sera from messenger RNA lipid nanoparticle immunizations blocked parasite transmission.

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Metadata

Authors
Dietrich, M. H., Chmielewski, J., Chan, L.-J., Tan, L. L., Adair, A., Lyons, F. M. T., Gabriela, M., Lopaticki, S., Dite, T. A., Dagley, L. F., Pazzagli, L., Gupta, P., Kamil, M., Vaughan, A. M., Rojrung, R., Abraham, A., Mazhari, R., Longley, R. J., Zeglinski, K., Gouil, Q., Mueller, I., Fabb, S. A., Shandre-Mugan, R., Pouton, C. W., Glukhova, A., Shakeel, S., & Tham, W.-H.
Affiliations
  • The University of Melbourne (AU)
  • Walter and Eliza Hall Institute of Medical Research (AU)
  • Seattle Children's Research Institute (US)
  • University of Washington (US)
  • Ehime University (JP)
  • Monash University (AU)
  • Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Australia.
  • Australian National University (AU)
Corresponding author
Tham, Wai-Hong
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2025-09-11
Volume
389
Issue
6765
Pages
eady0241-eady0241
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.ady0241
OpenAlex
W4412794604
Cited by
17
References
1
Citations by year
2026: 12 · 2025: 5
FWCI
15.48
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Science (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • ANU Open Research (Australian National University) (submittedVersion)
Topics
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Immunology and Microbiology › Parasitology › Bird parasitology and diseases
Keywords
Plasmodium falciparum, Pfs230, Pfs48/45, mosquito midgut, oocyst formation, malaria transmission blocking, nanobodies, epitope mapping, naturally acquired immunity
MeSH terms
Protein Domains, Animals, Anopheles, Antibodies, Protozoan, Epitopes, Antigens, Protozoan, Female, Fertilization, Immune Sera, Male, Membrane Glycoproteins, Mice, Inbred C57BL, Plasmodium falciparum, Protozoan Proteins, Malaria, Falciparum, Cryoelectron Microscopy, Oocysts, Mice, Nanoparticles

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