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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Structural basis for recognition of the malaria vaccine candidate Pfs48/45 by a transmission blocking antibody Frank Lennartz , Florian Brod , Rebecca Dabbs , Kazutoyo Miura , David Mekhaiel , Arianna Marini , Matthijs Jore , Max M. Søgaard , Thomas Jørgensen , Willem A. De Jongh , Robert W. Sauerwein , Carole A. Long , Sumi Biswas , Matthew Higgins Nature Communications 9 DOI: 10.1038/s41467-018-06340-9 Diamond Proposal Number(s): [18069] Open Access Show Abstract ▼ Abstract: The quest to develop an effective malaria vaccine remains a major priority in the fight against global infectious disease. An approach with great potential is a transmission-blocking vaccine which induces antibodies that prevent establishment of a productive infection in mosquitos that feed on infected humans, thereby stopping the transmission cycle. One of the most promising targets for such a vaccine is the gamete surface protein, Pfs48/45. Here we establish a system for production of full-length Pfs48/45 and use this to raise a panel of monoclonal antibodies. We map the binding regions of these antibodies on Pfs48/45 and correlate the location of their epitopes with their transmission-blocking activity. Finally, we present the structure of the C-terminal domain of Pfs48/45 bound to the most potent transmission-blocking antibody, and provide key molecular information for future structure-guided immunogen design.	Sep 2018

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