Like other retroviruses, HTLV-1 hijacks the CRM1/XPO1-dependent export pathway to transport its genomic RNA into the cytoplasm and continue its replication cycle. In a paper published in Nucleic Acids Research, scientists show that this hijacking affects the localization of the helicase UPF1 and blocks its activity in RNA degradation pathways, thereby impairing its antiviral function against viral RNA. More than a simple inhibition, this process redirects UPF1 toward proviral functions that ultimately enhance infection of neighboring cells.

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Reference

Prochasson L, Mghezzi-Habellah M, Roisin A, Palma M, Robin JP, de Bossoreille S, Cluet D, Mouelhi M, Decimo D, Desrames A, Chaze T, Matondo M, Dutartre H, Thoulouze MI, Lejeune F, Jalinot P, Rety S, Mocquet V. Retroviral adapters hijack the RNA helicase UPF1 in a CRM1/XPO1-dependent manner and reveal proviral roles of UPF1. Nucleic Acids Res. 2025 May 10;53(9):gkaf434. PMID: 40396490; PMCID: PMC12093142.

Doi: 10.1093/nar/gkaf434