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Updated: May 2, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
The C-terminal repeat domains of nsP3 from the Old World alphaviruses bind directly to G3BP
Marc D Panas1, Tero Ahola, Gerald M McInerney
1Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
Abstract:
The Old World alphaviruses block stress granule assembly by sequestration of RasGAP SH3-domain binding protein (G3BP). Here, we show that the proline-rich sequences in the hypervariable domain of nonstructural protein 3 (nsP3) of both Semliki Forest virus and Chikungunya virus were dispensable for binding to G3BP. nsP3 variants with or without this domain colocalized with G3BP. Furthermore, we show that the C-terminal repeat motifs of nsP3 were sufficient for G3BP binding.
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