EAP45 association with budding HIV-1: Kinetics and domain requirements.
| Autor: | Meng B; Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge, UK., Vallejo Ramirez PP; Laser Analytics Group, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK., Scherer KM; Laser Analytics Group, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK., Bruggeman E; Laser Analytics Group, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK., Kenyon JC; Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge, UK.; Department of Microbiology and Immunology, National University of Singapore, Singapore, Singapore.; Homerton College, University of Cambridge, Cambridge, UK., Kaminski CF; Laser Analytics Group, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK., Lever AM; Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge, UK.; Department of Medicine, National University of Singapore, Singapore, Singapore. |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | Traffic (Copenhagen, Denmark) [Traffic] 2021 Dec; Vol. 22 (12), pp. 439-453. Date of Electronic Publication: 2021 Oct 03. |
| DOI: | 10.1111/tra.12820 |
| Abstrakt: | A number of viruses including HIV use the ESCRT system to bud from the infected cell. We have previously confirmed biochemically that ESCRT-II is involved in this process in HIV-1 and have defined the molecular domains that are important for this. Here, using SNAP-tag fluorescent labelling and both fixed and live cell imaging we show that the ESCRT-II component EAP45 colocalises with the HIV protein Gag at the plasma membrane in a temporal and quantitative manner, similar to that previously shown for ALIX and Gag. We show evidence that a proportion of EAP45 may be packaged within virions, and we confirm the importance of the N terminus of EAP45 and specifically the H0 domain in this process. By contrast, the Glue domain of EAP45 is more critical for recruitment during cytokinesis, emphasising that viruses have ways of recruiting cellular components that may be distinct from those used by some cellular processes. This raises the prospect of selective interference with the pathway to inhibit viral function while leaving cellular functions relatively unperturbed. (© 2021 The Authors. Traffic published by John Wiley & Sons Ltd.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|