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Potent transmission-blocking monoclonal antibodies from naturally exposed individuals target a conserved epitope on Plasmodium falciparum Pfs230. 2023
Danton Ivanochko, and
Amanda Fabra-García, and
Karina Teelen, and
Marga van de Vegte-Bolmer, and
Geert-Jan van Gemert, and
Jocelyn Newton, and
Anthony Semesi, and
Marloes de Bruijni, and
Judith Bolscher, and
Jordache Ramjith, and
Marta Szabat, and
Stefanie Vogt, and
Lucas Kraft, and
Sherie Duncan, and
Shwu-Maan Lee, and
Moses R Kamya, and
Margaret E Feeney, and
Prasanna Jagannathan, and
Bryan Greenhouse, and
Robert W Sauerwein, and
C Richter King, and
Randall S MacGill, and
Teun Bousema, and
Matthijs M Jore, and
Jean-Philippe Julien
Program in Molecular Medicine, the Hospital for Sick Children Research Institute, Toronto, ON, Canada.
Pfs230 is essential for Plasmodium falciparum transmission to mosquitoes and is the protein targeted by the most advanced malaria-transmission-blocking vaccine candidate. Prior understanding of functional epitopes on Pfs230 is based on two monoclonal antibodies (mAbs) with moderate transmission-reducing activity (TRA), elicited from subunit immunization. Here, we screened the B cell repertoire of two naturally exposed individuals possessing serum TRA and identified five potent mAbs from sixteen Pfs230 domain-1-specific mAbs. Structures of three potent and three low-activity antibodies bound to Pfs230 domain 1 revealed four distinct epitopes. Highly potent mAbs from natural infection recognized a common conformational epitope that is highly conserved across P. falciparum field isolates, while antibodies with negligible TRA derived from natural infection or immunization recognized three distinct sites. Our study provides molecular blueprints describing P. falciparum TRA, informed by contrasting potent and non-functional epitopes elicited by natural exposure and vaccination.
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