The prehistoric fauna of Block Island, as indicated by its ancient shell heaps

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Abstract

SUMMARY

Circumsporozoite protein of the human malaria parasite Plasmodium falciparum (PfCSP) is the main target of antibodies that prevent the infection and disease. Protective antibodies recognize the central PfCSP domain, but our understanding of how parasite inhibition is associated with recognition of this domain and with the evolution of potent antibodies remains scattered. Here, we characterized the epitope specificity of 200 human monoclonal PfCSP antibodies. We show that the majority of PfCSP antibodies bind to NANP and NANP-like motifs with different preferences and define the molecular basis for recognition. Epitope cross-reactivity evolved with increasing antibody affinity around a conserved (N/D)P-NANP-N(V/A) core. High affinity to this motif, but not binding to NANP-like motifs, was associated with parasite inhibition and protection. Thus, NANP drives the development of potent PfCSP antibodies independently of their cross-reactivity profile, a finding with direct implications for the design of a second-generation PfCSP-based malaria vaccine.

HIGHLIGHTS

The majority of human PfCSP antibodies recognize multiple epitopes NANP affinity maturation drives the evolution of cross-reactive PfCSP antibodies Preferential PfCSP antibody binding to a conserved core motif High affinity not epitope specificity is associated with PfCSP antibody potency
Reference Key
openalex_W2328515687 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors G. F. Eaton
Journal american journal of science
Year 1898
DOI
10.2475/ajs.s4-6.32.137
URL
https://doi.org/10.2475/ajs.s4-6.32.137
Keywords Keywords not found

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