ArticleiScience2022
Structural dynamics reveal isolate-specific differences at neutralization epitopes on HIV Env.
Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Conformational landscape of HIV-1 Env from closed to fully open.Nature communications · 2026Article
- Vaccine elicitation of HIV-1 neutralizing antibodies against both V2 apex and fusion peptide in rhesus macaques.Cell reports · 2026Article
- Vaccine Elicitation of HIV-1 Neutralizing Antibodies Against Both V2 Apex and Fusion Peptide in Rhesus Macaques.bioRxiv : the preprint server for biology · 2025Article
- Unleashing virus structural biology: Probing protein and membrane intermediates in the dynamic process of membrane fusion.QRB discovery · 2025Review
- Neutralizing antibodies elicited in macaques recognize V3 residues on altered conformations of HIV-1 Env trimer.NPJ vaccines · 2024Article
- Microsecond dynamics control the HIV-1 Envelope conformation.Science advances · 2024Article
- Antibody Binding Captures High Energy State of an Antigen: The Case of Nsp1 SARS-CoV-2 as Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry.International journal of molecular sciences · 2023Article
- Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- Article
- Article
- Structure-Based Stabilization of SOSIP Env Enhances Recombinant Ectodomain Durability and Yield.Journal of virology · 2023Article
- An HIV-1 broadly neutralizing antibody overcomes structural and dynamic variation through highly focused epitope targeting.Npj viruses · 2023Article
- Antibody Recognition of CD4-Induced Open HIV-1 Env Trimers.Journal of virology · 2022Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
The envelope glycoprotein (Env) is the sole target for neutralizing antibodies against HIV and the most rapidly evolving, variable part of the virus. High-resolution structures of Env trimers captured in the pre-fusion, closed conformation have revealed a high degree of structural similarity across diverse isolates. Biophysical data, however, indicate that Env is highly dynamic, and the level of dynamics and conformational sampling is believed to vary dramatically between HIV isolates. Dynamic differences likely influence neutralization sensitivity, receptor activation, and overall trimer stability. Here, using hydrogen/deuterium-exchange mass spectrometry (HDX-MS), we have mapped local dynamics across native-like Env SOSIP trimers from diverse isolates. We show that significant differences in epitope order are observed across most sites targeted by broadly neutralizing antibodies. We also observe isolate-dependent conformational switching that occurs over a broad range of timescales. Lastly, we report that hyper-stabilizing mutations that dampen dynamics in some isolates have little effect on others.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.