What is it about?
Using high-resolution mass spectrometry, we identified - directly from the blood of a malaria-exposed child- the complete amino-acid sequence of a broadly inhibitory antibody that blocks the parasite’s key virulence protein, PfEMP1, from binding to the human endothelial protein C receptor (EPCR). This is the first demonstration that a functional, naturally acquired antibody can be sequenced straight from plasma without first isolating B cells.
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Why is it important?
Severe malaria is driven by infected red blood cells adhering to blood-vessel walls through PfEMP1, leading to organ damage and death. People living in endemic regions gradually acquire antibodies that prevent this binding. By pinpointing the exact antibody and showing how it recognizes conserved sites across many PfEMP1 variants, we reveal a clear target for vaccines or therapeutic antibodies aimed at stopping the deadliest form of malaria. The same approach can be extended to other infectious diseases where we need to understand the function and makeup of naturally acquired antibodies to the pathogen.
Perspectives
Together with our earlier discovery of broadly inhibitory antibodies isolated by B-cell sorting (Turner et al., Nature 2024), these findings suggest that such ‘magical’ monoclonal antibodies against malaria may be more common than previously thought and could provide powerful guidance for the design of next-generation malaria vaccines
Thomas Lavstsen
University of Copenhagen
Read the Original
This page is a summary of: Identification of broadly inhibitory anti-PfEMP1 antibodies by mass spectrometry sequencing of plasma IgG from a malaria-exposed child, Proceedings of the National Academy of Sciences, August 2025, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2508744122.
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