EAP45 association with budding HIV-1: Kinetics and domain requirements.
Vallejo Ramirez, Pedro P
Kenyon, Julia C
Traffic (Copenhagen, Denmark)
John Wiley and Sons
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Meng, B., Vallejo Ramirez, P. P., Scherer, K., Bruggeman, E., Kenyon, J. C., Kaminski, C., & Lever, A. (2021). EAP45 association with budding HIV-1: Kinetics and domain requirements.. Traffic (Copenhagen, Denmark) https://doi.org/10.1111/tra.12820
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.
Research Visit Grant by the Microbiology Society (BM), Gates Cambridge Scholarship (PVR), UK Medical Research Council (MRC) Grant (MR/N0229939/1)(JCK and AMLL), MRC Grants (MR/K015850/1 and MR/K02292X/1)(CFK), UK Engineering and Physical Sciences Research Council, EPSRC Grants (EP/L015889/1 and EP/H018301/1)(CFK), Wellcome Trust Grants (203249/Z/16/Z and 089703/Z/09/Z)(CFK), MedImmune, the RCUK under the Technology Touching Life Initiative, and Infinitus China Ltd (CFK).
Wellcome Trust (089703/Z/09/Z)
Wellcome Trust (203249/Z/16/Z)
Embargo Lift Date
External DOI: https://doi.org/10.1111/tra.12820
This record's URL: https://www.repository.cam.ac.uk/handle/1810/328657
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