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Updated: Mar 8, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
The HIV-1 envelope glycoprotein structure: nailing down a moving target
Andrew B Ward1, Ian A Wilson1,2
1Department of Integrative Structural and Computational Biology, International AIDS Vaccine Initiative Neutralizing Antibody Center, Collaboration for AIDS Vaccine Discovery, and Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, La Jolla, CA, USA.
High-resolution structures of the HIV-1 envelope glycoprotein (Env) reveal its complex glycan shield and plasticity. These insights enable the design of novel immunogens for developing effective HIV vaccines.
Area of Science:
- Structural biology
- Virology
- Immunology
Background:
- The HIV-1 envelope glycoprotein (Env) structure is crucial for viral entry and a key target for vaccines.
- Previous structure determination efforts faced challenges due to Env's complexity and instability.
Purpose of the Study:
- To present high-resolution structural data of HIV-1 Env trimers.
- To elucidate the role of the glycan shield and Env plasticity in antibody recognition and neutralization.
Main Methods:
- Cryo-electron microscopy (cryo-EM) and X-ray crystallography were used to determine Env structures.
- Analysis of Env-antibody complexes provided insights into epitope accessibility.
Main Results:
- High-resolution structures of SOSIP and native full-length Env trimers have been determined.
- The glycan shield's role and Env's inherent plasticity were revealed.
- Most Env surface epitopes, including neutralizing ones, involve both peptide and glycan components.
Conclusions:
- Structural insights into HIV-1 Env facilitate the design of stabilized trimers and immunogens.
- These advances have led to the development of vaccine-induced neutralizing antibodies.
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