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Structural and biophysical correlation of anti-NANP antibodies with in vivo protection against P. falciparum

The most advanced P. falciparum circumsporozoite protein (PfCSP)-based malaria vaccine confers partial protection. Here, Pholcharee et al. present crystal structures, binding affinities/kinetics, and in vivo protection of 8 anti-NANP antibodies to understand in vivo protection of PfCSP-targeting antibodies.

Tossapol Pholcharee
David Oyen
Ian A. Wilson
ResearchOpen Access16 Feb 2021
Nature Communications

Volume: 12, P: 1-14
Characterization of two non-competing antibodies to influenza H3N2 hemagglutinin stem reveals its evolving antigenicity

Structural characterization of two influenza hemagglutinin stem antibodies reveals binding to non-competing epitopes and the evolution of antigenicity of the hemagglutinin stem, which is a target for developing broadly protective influenza vaccines.

Akshita B. Gopal
Huibin Lv
Nicholas C. Wu
ResearchOpen Access26 Nov 2025
Nature Communications

Volume: 16, P: 1-12
Structural basis for DARC binding in reticulocyte invasion by Plasmodium vivax

Plasmodium vivax is one of the major causes of human malaria. To replicate, it must get inside human blood cells, in a processing requiring binding of the parasite PvDBP protein to the human DARC receptor. This study reveals how PvDBP binds to DARC and will guide future vaccine design.

Re’em Moskovitz
Tossapol Pholcharee
Matthew K. Higgins
ResearchOpen Access19 Jun 2023
Nature Communications

Volume: 14, P: 1-9
Affinity-matured homotypic interactions induce spectrum of PfCSP structures that influence protection from malaria infection

Here, the authors use cryo-EM to solve the structures of seven potent human antibodies, and demonstrate in vivo protection in a liver burden assay, using chimeric Plasmodium berghei sporozoites expressing Plasmodium falciparum circumsporozoite protein.

Gregory M. Martin
Jonathan L. Torres
Andrew B. Ward
ResearchOpen Access28 Jul 2023
Nature Communications

Volume: 14, P: 1-16
Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

The cryo-EM structure of the highly potent malaria antibody L9 reveals a key role of light-chain derived homotypic interactions in antigen binding and parasite inhibition, enabling antibody engineering and next-generation malaria vaccine design.

Gregory M. Martin
Monica L. Fernández-Quintero
Andrew B. Ward
ResearchOpen Access17 May 2023
Nature Communications

Volume: 14, P: 1-11

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Structural and biophysical correlation of anti-NANP antibodies with in vivo protection against P. falciparum

Characterization of two non-competing antibodies to influenza H3N2 hemagglutinin stem reveals its evolving antigenicity

Structural basis for DARC binding in reticulocyte invasion by Plasmodium vivax

Affinity-matured homotypic interactions induce spectrum of PfCSP structures that influence protection from malaria infection

Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

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Structural and biophysical correlation of anti-NANP antibodies with in vivo protection against P. falciparum

Characterization of two non-competing antibodies to influenza H3N2 hemagglutinin stem reveals its evolving antigenicity

Structural basis for DARC binding in reticulocyte invasion by Plasmodium vivax

Affinity-matured homotypic interactions induce spectrum of PfCSP structures that influence protection from malaria infection

Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

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