Structural principles controlling HIV envelope glycosylation
The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans...
| Main Authors: | , |
|---|---|
| Format: | Journal article |
| Published: |
Elsevier
2017
|
| _version_ | 1826306774482812928 |
|---|---|
| author | Behrens, A Crispin, M |
| author_facet | Behrens, A Crispin, M |
| author_sort | Behrens, A |
| collection | OXFORD |
| description | The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive ‘trimer-induced mannose patch’. Importantly, the immature glycans present a highly conserved feature of the virus that is targeted by broadly neutralizing antibodies. Quantitative mass spectrometry of glycopeptides together with structures of the trimeric viral-spike define the steric principles controlling processing and provide a detailed map of the glycan shield. |
| first_indexed | 2024-03-07T06:53:01Z |
| format | Journal article |
| id | oxford-uuid:fd2b89ea-0a38-456f-934f-6029c4682975 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T06:53:01Z |
| publishDate | 2017 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:fd2b89ea-0a38-456f-934f-6029c46829752022-03-27T13:26:50ZStructural principles controlling HIV envelope glycosylationJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fd2b89ea-0a38-456f-934f-6029c4682975Symplectic Elements at OxfordElsevier2017Behrens, ACrispin, MThe heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive ‘trimer-induced mannose patch’. Importantly, the immature glycans present a highly conserved feature of the virus that is targeted by broadly neutralizing antibodies. Quantitative mass spectrometry of glycopeptides together with structures of the trimeric viral-spike define the steric principles controlling processing and provide a detailed map of the glycan shield. |
| spellingShingle | Behrens, A Crispin, M Structural principles controlling HIV envelope glycosylation |
| title | Structural principles controlling HIV envelope glycosylation |
| title_full | Structural principles controlling HIV envelope glycosylation |
| title_fullStr | Structural principles controlling HIV envelope glycosylation |
| title_full_unstemmed | Structural principles controlling HIV envelope glycosylation |
| title_short | Structural principles controlling HIV envelope glycosylation |
| title_sort | structural principles controlling hiv envelope glycosylation |
| work_keys_str_mv | AT behrensa structuralprinciplescontrollinghivenvelopeglycosylation AT crispinm structuralprinciplescontrollinghivenvelopeglycosylation |