Author: Aravinth Kumar Jayabalan; Diane E. Griffin; Anthony K. L. Leung
Title: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation Document date: 2019_6_20
ID: n8sjpcbs_1
Snippet: Page 5 macrodomain (MD) in the N-terminus, a central zinc-binding domain, and a C-terminal hypervariable domain (HVD), which is of low-complexity [39] . Recent studies indicate that short peptide motifs within the HVD direct nsP3 binding to host SG proteins [39, 40, 43] . Specifically, two repeat peptide motifs within the HVD of the alphavirus chikungunya virus (CHIKV) bind to the essential SG components G3BP1 and G3BP2 [40, 44] . Given that the .....
Document: Page 5 macrodomain (MD) in the N-terminus, a central zinc-binding domain, and a C-terminal hypervariable domain (HVD), which is of low-complexity [39] . Recent studies indicate that short peptide motifs within the HVD direct nsP3 binding to host SG proteins [39, 40, 43] . Specifically, two repeat peptide motifs within the HVD of the alphavirus chikungunya virus (CHIKV) bind to the essential SG components G3BP1 and G3BP2 [40, 44] . Given that the expression of alphaviral nsP3 alone suppresses SG formation and nsP3 expression increases over the course of viral infection, it was proposed that nsP3 sequesters G3BP1/2 resulting in SG disassembly during the late phase of infection [35, 36, 41] .
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