%0 Journal Article
%A Ko, Kuang-Ting
%A Lennartz, Frank
%A Mekhaiel, David
%A Guloglu, Bora
%A Marini, Arianna
%A Deuker, Danielle J.
%A Long, Carole A.
%A Jore, Matthijs M.
%A Miura, Kazutoyo
%A Biswas, Sumi
%A Higgins, Matthew K.
%T Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies
%J Nature Communications
%V 13
%N 1
%@ 2041-1723
%C [London]
%I Nature Publishing Group UK
%M PUBDB-2022-06895
%P 5603
%D 2022
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:36153317
%U <Go to ISI:>//WOS:000858076500002
%R 10.1038/s41467-022-33379-6
%U https://bib-pubdb1.desy.de/record/485846