Please use this identifier to cite or link to this item: https://doi.org/10.1111/tra.12820
Title: EAP45 association with budding HIV-1: Kinetics and domain requirements
Authors: Meng, Bo
Vallejo Ramirez, P.P.
Scherer, Katharina M.
Bruggeman, Ezra
Kenyon, Julia C. 
Kaminski, Clemens F.
Lever, Andrew M. 
Keywords: budding
colocalisation
ESCRT
gag
HIV
TIRF
Issue Date: 3-Oct-2021
Publisher: John Wiley and Sons Inc
Citation: Meng, Bo, Vallejo Ramirez, P.P., Scherer, Katharina M., Bruggeman, Ezra, Kenyon, Julia C., Kaminski, Clemens F., Lever, Andrew M. (2021-10-03). EAP45 association with budding HIV-1: Kinetics and domain requirements. Traffic 22 (12) : 439-453. ScholarBank@NUS Repository. https://doi.org/10.1111/tra.12820
Rights: Attribution 4.0 International
Abstract: 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.
Source Title: Traffic
URI: https://scholarbank.nus.edu.sg/handle/10635/232194
ISSN: 1398-9219
DOI: 10.1111/tra.12820
Rights: Attribution 4.0 International
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