期刊
CELL
卷 178, 期 1, 页码 216-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2019.05.025
关键词
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资金
- European Union [305282, 733273]
- Wellcome Trust [206194, 104923/Z/14/Z, 105399/Z/14/Z, 201477/Z/16/Z, 101020/Z/13/Z, 106917/Z/15/Z]
- United States Agency for International Development (USAID)
- NIH, National Institute of Allergy and Infectious Diseases
- UK MRC programme [MR/N020413/1]
- NHMRC [1092789]
- UK MRC iCASE PhD Studentships [MR/K017632/1, MR/N013468/1]
- Wellcome Trust [105399/Z/14/Z, 201477/Z/16/Z, 104923/Z/14/Z] Funding Source: Wellcome Trust
- MRC [1808501, MR/N020413/1, MR/K025554/1] Funding Source: UKRI
- National Health and Medical Research Council of Australia [1092789] Funding Source: NHMRC
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [ZIAAI001020] Funding Source: NIH RePORTER
The Plasmodium falciparum reticulocyte-binding protein homolog 5 (PfRH5) is the leading target for next-generation vaccines against the disease-causing blood-stage of malaria. However, little is known about how human antibodies confer functional immunity against this antigen. We isolated a panel of human monoclonal antibodies (mAbs) against PfRH5 from peripheral blood B cells from vaccinees in the first clinical trial of a PfRH5-based vaccine. We identified a subset of mAbs with neutralizing activity that bind to three distinct sites and another subset of mAbs that are non-functional, or even antagonistic to neutralizing antibodies. We also identify the epitope of a novel group of non-neutralizing antibodies that significantly reduce the speed of red blood cell invasion by the merozoite, thereby potentiating the effect of all neutralizing PfRH5 antibodies as well as synergizing with antibodies targeting other malaria n proteins. Our results provide a roadmap for structure-guided vaccine development to maximize antibody efficacy against blood-stage malaria.
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