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Showing 1–5 of 5 results
Advanced filters: Author: Anthony Semesi Clear advanced filters

  • Several transmission-blocking vaccine candidates based on Pfs230 and Pfs48/45 are in clinical development, but it remains unclear whether they will demonstrate high efficacy. Here, the authors develop a stabilized chimeric antigen presenting potent epitopes from Pfs230 and Pfs48/45 in a single construct and demonstrate induction of transmission-reducing antibodies when female mice are immunized with the antigen in a self-assembling protein nanoparticle formulation.

    • Danton Ivanochko
    • Kazutoyo Miura
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-16

  • Malaria protein Pfs48/45 is a promising transmission-blocking antigen targeted by antibodies. Here, the authors determine the structure of its transmission-blocking epitope I, and generate a humanized monoclonal antibody that binds Pfs48/45 with high affinity.

    • Prasun Kundu
    • Anthony Semesi
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-9

  • Kucharska, Ivanochko and Hailemariam and colleagues solved cryo-EM structures of Pfs48/45, needed for Plasmodium falciparum development, with potent antibodies. The work revealed conformational epitopes, with implications for design of therapies against malaria.

    • Iga Kucharska
    • Danton Ivanochko
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1396-1407

  • Here, the authors combine three different antibody specificities and an Fc domain on a single multivalent molecule, resulting in high neutralization activity despite viral sequence variability.

    • Edurne Rujas
    • Iga Kucharska
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • The inducible co-stimulator (ICOS) is a member of the CD28/B7 superfamily, binding its ligand (ICOS-L) on activated T cells. The structure of the ICOS/ICOS-L complex reveals a distinct receptor binding orientation. The structures of ICOS and ICOS-L in complex with potentially therapeutic antibodies suggest the structural basis of such antibodies’ efficacies and high binding affinities.

    • Edurne Rujas
    • Hong Cui
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11