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Retroviral adapters hijack the RNA helicase UPF1 in a CRM1/XPO1-dependent manner and reveal proviral roles of UPF1.
Nucleic Acids Res, 53(9).
The hijacking of CRM1 export is an important step of the retroviral replicationcycle. Here, we investigated the consequences of this hijacking for the host.During HTLV-1 infection, we identified that this hijacking by the viral proteinRex favours the association between CRM1 and the RNA helicase UPF1, leading to adecreased affinity of UPF1 for cellular RNA and its nuclear retention. As aconsequence, we found that the nonsense-mediated mRNA decay (NMD), known to havean antiviral function, was inhibited. Corroborating these results, we described asimilar process with Rev, the functional homolog of Rex from HIV-1. Unexpectedly,we also found that, for HTLV-1, this process is coupled with the specific loadingof UPF1 onto vRNA, independently of NMD. In this latter context, UPF1 positivelyregulates several steps of the viral replication cycle, from the nuclear exportof vRNA to the production of mature viral particles.
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