1. A high affinity human monoclonal antibody against Pfs230 binds multiple parasite stages and blocks oocyst formation in mosquitoes
- Author
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Jian Han, David L. Narum, Wanhu Tang, Johannes Trück, Miranda Byrne-Steele, Nichole D. Salinas, Brittany Brown, Raul Herrera, Karine Reiter, Margery G. Smelkinson, Joel Vega-Rodríguez, Justin J. Taylor, Pan W, Richard L. Shimp, Doritchamou Jya, Issaka Sagara, Jacob D. Galson, Silva TLAe, Camila H. Coelho, Mary Eisenhower, Patrick E. Duffy, Martin Burkhardt, Jonathan P. Renn, Nguyen, Niraj H. Tolia, Olga Muratova, Nicholas J. MacDonald, Bethany J Jenkins, and Hou X
- Subjects
biology ,Transmission (medicine) ,medicine.drug_class ,B-cell receptor ,medicine.disease ,Monoclonal antibody ,Virology ,medicine.anatomical_structure ,Malaria elimination ,parasitic diseases ,biology.protein ,medicine ,Parasite hosting ,Gamete ,Antibody ,Malaria - Abstract
Malaria elimination requires tools that interrupt parasite transmission. Here, we characterized B cell receptor responses among Malian adults vaccinated against the first domain of the cysteine-rich 230kDa gamete surface protein Pfs2301–3 to neutralize sexual stage P. falciparum parasites and halt their further spread. We generated nine Pfs230 human monoclonal antibodies (mAbs). One mAb potently blocked transmission to mosquitoes in a complement-dependent manner and reacted strongly to gamete surface while eight mAbs showed only low or no blocking activity. This study provides a rational basis to improve malaria vaccines and develop therapeutic antibodies for malaria elimination.
- Published
- 2020