Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies.

• Tác giả: Carolina M Andrade, Ezra T Bekkering, Teun Bousema, Sophia Hailemariam, Fabian Heide, Maartje R Inklaar, Danton Ivanochko, Matthew Jackman, Pascal W T C Jansen, Matthijs M Jore, Jean-Philippe Julien, Taco W A Kooij, Nicholas I Proellochs, John L Rubinstein, Rianne Stoter, Renate C van Daalen, Michiel Vermeulen, Oscar T Wanders, Randy Yoo
• Ngôn ngữ: eng
• Ký hiệu phân loại: 005.113 Structured programming
• Thông tin xuất bản: United States : bioRxiv : the preprint server for biology , 2025
• Bộ sưu tập: NCBI
• ID: 673657

Tóm tắt

The Pfs230:Pfs48/45 complex is essential for malaria parasites to infect mosquitoes and forms the basis for current leading 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