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Garvanska, Dimitriya H; Alvarado, R Elias; Mundt, Filip Oskar; Lindqvist, Richard; Duel, Josephine Kerzel; Coscia, Fabian; Nilsson, Emma; Lokugamage, Kumari; Johnson, Bryan A; Plante, Jessica A; Morris, Dorothea R; Vu, Michelle N; Estes, Leah K; McLeland, Alyssa M; Walker, Jordyn; Crocquet-Valdes, Patricia A; Mendez, Blanca Lopez; Plante, Kenneth S; Walker, David H; Weisser, Melanie Bianca; Överby, Anna K; Mann, Matthias; Menachery, Vineet D; Nilsson, Jakob
EMBO reports, 02/2024, Letnik: 25, Številka: 2Journal Article
Viruses interact with numerous host factors to facilitate viral replication and to dampen antiviral defense mechanisms. We currently have a limited mechanistic understanding of how SARS-CoV-2 binds host factors and the functional role of these interactions. Here, we uncover a novel interaction between the viral NSP3 protein and the fragile X mental retardation proteins (FMRPs: FMR1, FXR1-2). SARS-CoV-2 NSP3 mutant viruses preventing FMRP binding have attenuated replication in vitro and reduced levels of viral antigen in lungs during the early stages of infection. We show that a unique peptide motif in NSP3 binds directly to the two central KH domains of FMRPs and that this interaction is disrupted by the I304N mutation found in a patient with fragile X syndrome. NSP3 binding to FMRPs disrupts their interaction with the stress granule component UBAP2L through direct competition with a peptide motif in UBAP2L to prevent FMRP incorporation into stress granules. Collectively, our results provide novel insight into how SARS-CoV-2 hijacks host cell proteins and provides molecular insight into the possible underlying molecular defects in fragile X syndrome. Synopsis The SARS-CoV-2 NSP3 protein binds directly to fragile X mental retardation proteins (FMRPs) to support viral replication. NSP3 binding disrupts FMRP interaction with the stress granule protein UBAP2L, thereby preventing FMRP localization to these structures. The SARS-CoV-2 NSP3 protein binds to the KH domains of FMRPs through a short peptide motif. Engineered SARS-CoV-2 viruses unable to bind FMRPs have reduced replication. NSP3 binding to FMRPs disrupts their localization to stress granules through competition with UBAP2L. The SARS-CoV-2 NSP3 protein binds directly to fragile X mental retardation proteins (FMRPs) to support viral replication. NSP3 binding disrupts FMRP interaction with the stress granule protein UBAP2L, thereby preventing FMRP localization to these structures.
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