Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state
One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry its exact role during the first ste...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
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Cell Press
2017
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| _version_ | 1826303169286635520 |
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| author | Jones, D Alvarez, L Nolan, R Ferriz, M Sainz Urruela, R Massana-Munoz, X Novak-Kotzer, H Dustin, M Padilla Parra, S |
| author_facet | Jones, D Alvarez, L Nolan, R Ferriz, M Sainz Urruela, R Massana-Munoz, X Novak-Kotzer, H Dustin, M Padilla Parra, S |
| author_sort | Jones, D |
| collection | OXFORD |
| description | One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry its exact role during the first steps of HIV-1 infection is not well characterized. Here, we utilised a multidisciplinary approach to study the DNM2 role during fusion of HIV-1 in primary resting CD4 T and TZM-bl cells. We have combined advanced light microscopy and functional cell- based assays to experimentally assess the role of dynamin-2 during these processes. Overall our data suggests that dynamin 2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion. |
| first_indexed | 2024-03-07T05:58:34Z |
| format | Journal article |
| id | oxford-uuid:eb634554-6c7d-4a30-9e01-16c036ee23ad |
| institution | University of Oxford |
| last_indexed | 2024-03-07T05:58:34Z |
| publishDate | 2017 |
| publisher | Cell Press |
| record_format | dspace |
| spelling | oxford-uuid:eb634554-6c7d-4a30-9e01-16c036ee23ad2022-03-27T11:09:15ZDynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric stateJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:eb634554-6c7d-4a30-9e01-16c036ee23adSymplectic Elements at OxfordCell Press2017Jones, DAlvarez, LNolan, RFerriz, MSainz Urruela, RMassana-Munoz, XNovak-Kotzer, HDustin, MPadilla Parra, SOne of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry its exact role during the first steps of HIV-1 infection is not well characterized. Here, we utilised a multidisciplinary approach to study the DNM2 role during fusion of HIV-1 in primary resting CD4 T and TZM-bl cells. We have combined advanced light microscopy and functional cell- based assays to experimentally assess the role of dynamin-2 during these processes. Overall our data suggests that dynamin 2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion. |
| spellingShingle | Jones, D Alvarez, L Nolan, R Ferriz, M Sainz Urruela, R Massana-Munoz, X Novak-Kotzer, H Dustin, M Padilla Parra, S Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title | Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title_full | Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title_fullStr | Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title_full_unstemmed | Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title_short | Dynamin-2 stabilizes the HIV-1 fusion pore with a low oligomeric state |
| title_sort | dynamin 2 stabilizes the hiv 1 fusion pore with a low oligomeric state |
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