HIV-1 Envelope Conformation, Allostery, and Dynamics.
The HIV-1 envelope glycoprotein (Env) mediates host cell fusion and is the primary target for HIV-1 vaccine design. The Env undergoes a series of functionally important conformational rearrangements upon engagement of its host cell receptor, CD4. As the sole target for broadly neutralizing antibodies, our understanding of these transitions plays a critical role in vaccine immunogen design. Here, we review available experimental data interrogating the HIV-1 Env conformation and detail computational efforts aimed at delineating the series of conformational changes connecting these rearrangements. These studies have provided a structural mapping of prefusion closed, open, and transition intermediate structures, the allosteric elements controlling rearrangements, and state-to-state transition dynamics. The combination of these investigations and innovations in molecular modeling set the stage for advanced studies examining rearrangements at greater spatial and temporal resolution.
Duke Scholars
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Related Subject Headings
- env Gene Products, Human Immunodeficiency Virus
- Virus Internalization
- Protein Multimerization
- Protein Conformation
- Protein Binding
- Models, Molecular
- HIV-1
- HIV Envelope Protein gp41
- HIV Antibodies
- Antibodies, Neutralizing
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Location
Related Subject Headings
- env Gene Products, Human Immunodeficiency Virus
- Virus Internalization
- Protein Multimerization
- Protein Conformation
- Protein Binding
- Models, Molecular
- HIV-1
- HIV Envelope Protein gp41
- HIV Antibodies
- Antibodies, Neutralizing