biostudies-literatureLavender AAUS Department of Education, GAANN fellowshipNIAID NIH HHSYerkes National Primate Research Center, Emory UniversityNational Institutes of HealthGSU Molecular Basis of Disease FellowshipNIH HHSe0079425https://www.ebi.ac.uk/biostudies/studies/S-EPMC12282152biostudies-literatureUnknown99(7)Stress granules (SGs) are dynamic, cytoplasmic foci that form in response to environmental stresses, including viral infections, and function to restore cellular homeostasis by regulating mRNA translation, storage, and decay. To inhibit SG formation and subvert their antiviral effects, viruses from diverse families sequester or cleave G3BP1, the key SG nucleating protein. We found that an infection with simian hemorrhagic fever virus (SHFV), a member of the family <i>Arteriviridae</i>, does not induce the formation of <i>bona fide</i> SGs despite inducing phosphorylation of PKR and eIF2α. The SG proteins, G3BP1, G3BP2, TIA-1, Caprin-1, and USP10, but not the translation initiation proteins, eIF3A, eIF4G, and small ribosomal protein S6 (rpS6), were redistributed into foci located in the samJournal of virologyThe SHFV nsp2 and nucleocapsid proteins recruit G3BP1 to sites of viral replication, but stress granules are not induced by the infection.PMC12282152P51 OD011132P51OD011132, U42PDP11023R21 AI073824AI073824Peck HEBrinton MATang H-YLavender AAVanover DSantangelo PJSolanke OfalseThe SHFV nsp2 and nucleocapsid proteins recruit G3BP1 to sites of viral replication, but stress granules are not induced by the infection.Stress granules (SGs) are dynamic, cytoplasmic foci that form in response to environmental stresses, including viral infections, and function to restore cellular homeostasis by regulating mRNA translation, storage, and decay. To inhibit SG formation and subvert their antiviral effects, viruses from diverse families sequester or cleave G3BP1, the key SG nucleating protein. We found that an infection with simian hemorrhagic fever virus (SHFV), a member of the family <i>Arteriviridae</i>, does not induce the formation of <i>bona fide</i> SGs despite inducing phosphorylation of PKR and eIF2α. The SG proteins, G3BP1, G3BP2, TIA-1, Caprin-1, and USP10, but not the translation initiation proteins, eIF3A, eIF4G, and small ribosomal protein S6 (rpS6), were redistributed into foci located in the sam2025-01-01T00:00:00Z2025 Jul2025-08-27T03:06:38.62Z2025-08-21T09:53:17.132ZS-EPMC122821524054874210.1128/jvi.00794-25