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 antibodie...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-05-01
|
| Series: | Viruses |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1999-4915/13/5/852 |
| _version_ | 1797534984709341184 |
|---|---|
| author | Ashley Lauren Bennett Rory Henderson |
| author_facet | Ashley Lauren Bennett Rory Henderson |
| author_sort | Ashley Lauren Bennett |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T11:38:14Z |
| format | Article |
| id | doaj.art-171daf6f0e5c439490b462f60f0472be |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T11:38:14Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-171daf6f0e5c439490b462f60f0472be2023-11-21T18:41:00ZengMDPI AGViruses1999-49152021-05-0113585210.3390/v13050852HIV-1 Envelope Conformation, Allostery, and DynamicsAshley Lauren Bennett0Rory Henderson1Duke Human Vaccine Institute, Durham, NC 27710, USADuke Human Vaccine Institute, Durham, NC 27710, USAThe 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.https://www.mdpi.com/1999-4915/13/5/852HIV-1envelopeallosterymolecular dynamicsstructure |
| spellingShingle | Ashley Lauren Bennett Rory Henderson HIV-1 Envelope Conformation, Allostery, and Dynamics Viruses HIV-1 envelope allostery molecular dynamics structure |
| title | HIV-1 Envelope Conformation, Allostery, and Dynamics |
| title_full | HIV-1 Envelope Conformation, Allostery, and Dynamics |
| title_fullStr | HIV-1 Envelope Conformation, Allostery, and Dynamics |
| title_full_unstemmed | HIV-1 Envelope Conformation, Allostery, and Dynamics |
| title_short | HIV-1 Envelope Conformation, Allostery, and Dynamics |
| title_sort | hiv 1 envelope conformation allostery and dynamics |
| topic | HIV-1 envelope allostery molecular dynamics structure |
| url | https://www.mdpi.com/1999-4915/13/5/852 |
| work_keys_str_mv | AT ashleylaurenbennett hiv1envelopeconformationallosteryanddynamics AT roryhenderson hiv1envelopeconformationallosteryanddynamics |