Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies

Kuang-Ting Ko, Frank Lennartz, David Mekhaiel, Bora Guloglu, Arianna Marini, Danielle J. Deuker, Carole A. Long, Matthijs M. Jore, Kazutoyo Miura, Sumi Biswas () and Matthew K. Higgins ()
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Kuang-Ting Ko: South Parks Road, University of Oxford
Frank Lennartz: South Parks Road, University of Oxford
David Mekhaiel: University of Oxford
Bora Guloglu: South Parks Road, University of Oxford
Arianna Marini: University of Oxford
Danielle J. Deuker: University of Oxford
Carole A. Long: NIH
Matthijs M. Jore: Radboud University Medical Centre
Kazutoyo Miura: NIH
Sumi Biswas: University of Oxford
Matthew K. Higgins: South Parks Road, University of Oxford

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract An effective malaria vaccine remains a global health priority and vaccine immunogens which prevent transmission of the parasite will have important roles in multi-component vaccines. One of the most promising candidates for inclusion in a transmission-blocking malaria vaccine is the gamete surface protein Pfs48/45, which is essential for development of the parasite in the mosquito midgut. Indeed, antibodies which bind Pfs48/45 can prevent transmission if ingested with the parasite as part of the mosquito bloodmeal. Here we present the structure of full-length Pfs48/45, showing its three domains to form a dynamic, planar, triangular arrangement. We reveal where transmission-blocking and non-blocking antibodies bind on Pfs48/45. Finally, we demonstrate that antibodies which bind across this molecule can be transmission-blocking. These studies will guide the development of future Pfs48/45-based vaccine immunogens.

Date: 2022
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DOI: 10.1038/s41467-022-33379-6

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