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Updated: Feb 7, 2026
07:10
Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
Published on: September 14, 2014
14.7K
Structure-Guided Redesign Improves NFL HIV Env Trimer Integrity and Identifies an Inter-Protomer Disulfide Permitting
Lifei Yang1, Shailendra Kumar Sharma2, Christopher Cottrell1
1Department of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, United States.
Frontiers in Immunology
|August 2, 2018
Summary
New designs for soluble HIV-1 envelope glycoprotein (Env) trimers enhance stability and antigenicity. These native flexibly linked (NFL) trimers mimic the Env spike, improving vaccine potential by exposing key neutralizing epitopes.
Area of Science:
- Structural biology
- Immunology
- Virology
Background:
- Soluble HIV-1 envelope glycoprotein (Env) trimers are crucial vaccine candidates.
- Native flexibly linked (NFL) trimers mimic the native Env spike structure.
- Optimizing trimer stability and antigenicity is key for effective immunogens.
Purpose of the Study:
- To engineer novel, stable, and homogeneous HIV-1 NFL Env trimers.
- To explore modifications that enhance trimer integrity and expose key epitopes.
- To develop improved vaccine candidates based on HIV-1 Env structure.
Main Methods:
- Proline substitution screening in the gp41 heptad repeat 1 region.
- Structure-guided cysteine pair screening to form inter-protomer disulfide bonds.
- Engineering enterokinase cleavage sites for controlled fusion peptide exposure.
Main Results:
- Identified proline substitutions (e.g., L555P) enhancing trimer integrity.
- A specific cysteine pair (A501C-L663C) increased NFL trimer thermostability.
- Redesigned trimers showed enhanced stability, homogeneity, and exposure of neutralizing epitopes.
Conclusions:
- Novel HIV-1 Env trimers exhibit improved stability and antigenic properties.
- These engineered trimers present enhanced exposure of fusion peptide and interface epitopes.
- The study provides a framework for developing advanced HIV-1 Env-based immunogens.
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