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Showing 1–13 of 13 results
Advanced filters: Author: Priyamvada Acharya Clear advanced filters

  • In this study, Thakur et al determined cryo-EM structures of receptor-bound HIV-1 envelope (Env) to track how the fusion peptide transitions from being antibody accessible prior to receptor binding to becoming inaccessible in receptor-bound Env.

    • Bhishem Thakur
    • Revansiddha H. Katte
    • Priyamvada Acharya
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • In this study, Henderson and Zhou et al. visualize the development of a HIV-1 broadly neutralizing antibody (bnAb) from germline to maturity by determining cryo-EM structures of HIV-1 Envelope (Env) proteins bound to Fab fragments of antibodies at different stages of development of a Env V3-glcyan supersite targeting bnAb clone.

    • Rory Henderson
    • Ye Zhou
    • Priyamvada Acharya
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Here, using cryo-EM and smFRET, Henderson et al. show how tryptophan 571 in the HIV-1 Env acts as a conformational switch during receptor-mediated viral entry and design HIV-1 Env proteins that cannot undergo conformational changes. This has important implications for HIV-1 vaccine design.

    • Rory Henderson
    • Maolin Lu
    • S. Munir Alam
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • The SARS-CoV-2 spike glycoprotein is flexible, and its receptor-binding domain (RBD) fluctuates between up or down conformations. Mutations engineered into the spike ectodomain either lock the RBD in the down state or make it adopt the up conformation more readily.

    • Rory Henderson
    • Robert J. Edwards
    • Priyamvada Acharya
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 925-933

  • In this work, researchers engineer HIV-1 immunogens using molecular dynamics simulations to enhance vaccine designs that select for specific antibody mutations. Their approach improved the selection of mutations crucial for broadly neutralizing antibody responses, offering a promising strategy for HIV vaccine development.

    • Rory Henderson
    • Kara Anasti
    • Barton F. Haynes
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-20

  • HIV-1 is a formidable target for vaccine development. Here, Parthasarathy et al. show that envelope glycoproteins of some HIV-1 primary strains exhibit inherent conformational flexibility that may contribute to HIV-1 evasion from neutralizing antibodies.

    • Durgadevi Parthasarathy
    • Karunakar Reddy Pothula
    • Alon Herschhorn
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • The SARS-CoV-2 spike ectodomain is destabilized by cold temperature storage, an effect that can be reversed by incubation at 37 °C or by stabilizing its conformation in the ‘down’ state.

    • Robert J. Edwards
    • Katayoun Mansouri
    • Priyamvada Acharya
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 128-131

  • Immunization of macaques with nanoparticle-conjugated receptor-binding domain of SARS-CoV-2 adjuvanted with 3M-052 and alum results in cross-neutralizing antibodies against bat coronaviruses, SARS-CoV and SARS-CoV-2 variants, and may provide a platform for developing pan-coronavirus vaccines.

    • Kevin O. Saunders
    • Esther Lee
    • Barton F. Haynes
    Research
    Nature
    Volume: 594, P: 553-559

  • A crystal structure of the human immunodeficiency virus Env trimer, used by the virus to infect cells, is determined here; the new structure, which shows the pre-fusion form of Env, increases our understanding of the fusion mechanism and of how the conformation of Env allows the virus to evade the immune response.

    • Marie Pancera
    • Tongqing Zhou
    • Peter D. Kwong
    Research
    Nature
    Volume: 514, P: 455-461