2026-05-31T14:51:14Zhttps://riuma.uma.es/rest/oai/request

oai:riuma.uma.es:10630/170112026-02-03T11:48:44Zcom_10630_2254col_10630_37959

00925njm 22002777a 4500 dc Krenz, Björn author 2018-12-10 Plant viruses have the ability to redirect host machineries and processes to establish a productive infection. Virus-host interactions lead to the reprogramming of the plant cell cycle and transcriptional controls, inhibition of cell death pathways, interference with cell signaling and protein turnover, and suppression defense pathways. Stress granules (SGs) are structures within cells that regulate gene expression during stress response, e.g. viral infection. In mammalian cells assembly of SGs is dependent on the Ras-GAP SH3-domain–binding protein (G3BP). The C-terminal domain of the viral nonstructural protein 3 (nsP3) of Semliki Forest virus (SFV) forms a complex with mammalian G3BP and sequesters it into viral RNA replication complexes in a manner that inhibits the formation of SGs. The binding domain of nsP3 to HsG3BP was mapped to two tandem ‘FGDF’ repeat motifs close to the C-terminus of the viral proteins. It was speculated that plant viruses employ a similar strategy to inhibit SG function. https://hdl.handle.net/10630/17011 Virus Analyzing plant stress granules in response to plant viruses