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To counteract this host response, viruses have evolved a broad spectrum of strategies to inhibit SG formation. However, the molecular mechanisms underlying SG inhibition remain poorly understood. The nucleocapsid proteins play a critical role in virus replication and host interaction. Here, using Semliki Forest Virus (SFV) as a model, we uncover the function of the alphavirus nucleocapsid in SG inhibition. This inhibitory function depends on oligomerization mediated by an N\u2010terminal \u03b1\u2010helix and with a positively charged intrinsically disordered region (IDR). We show that SFV capsid directly competes with G3BP1 for RNA binding, thereby disrupting G3BP1\u2010RNA liquid\u2013liquid phase separation (LLPS) in vitro and SG assembly in cells. This mechanism is conserved across the alphavirus family but is not shared by the nucleocapsid of SARS\u2010CoV\u20102 or other endemic viruses examined. Notably, expression of a peptide from SFV capsid is sufficient to inhibit SG formation induced by Amyotrophic Lateral Sclerosis (ALS)\u2010associated mutations, suggesting potential therapeutic applications. Our findings reveal mechanistic insight into SG modulation by the viral capsid protein and provide a possible bioengineering tool for probing SG dynamics in health and disease.<\/jats:p>","DOI":"10.1002\/advs.202517009","type":"journal-article","created":{"date-parts":[[2026,1,27]],"date-time":"2026-01-27T15:24:11Z","timestamp":1769527451000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Alphaviral Capsid Proteins Inhibit Stress Granule Assembly via Competitive RNA Binding With G3BP1"],"prefix":"10.1002","volume":"13","author":[{"given":"Yun","family":"Zhang","sequence":"first","affiliation":[{"name":"School of Pharmacy Hangzhou Normal University  Hangzhou Zhejiang China"},{"name":"Westlake Laboratory of Life Sciences and Biomedicine School of Life Sciences Westlake University  Hangzhou Zhejiang 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Westlake University  Hangzhou Zhejiang China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ziqiu","family":"Wang","sequence":"additional","affiliation":[{"name":"Westlake Laboratory of Life Sciences and Biomedicine School of Life Sciences Westlake University  Hangzhou Zhejiang China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yiqiong","family":"Bao","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology School of Basic Medical Sciences Peking University Health Science Center  Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tingting","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology School of Basic Medical Sciences Peking University Health Science Center  Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoming","family":"Zhou","sequence":"additional","affiliation":[{"name":"Westlake Laboratory of Life Sciences and Biomedicine School of Life Sciences Westlake University  Hangzhou Zhejiang China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiabin","family":"Chen","sequence":"additional","affiliation":[{"name":"School of Pharmacy Hangzhou Normal University  Hangzhou Zhejiang China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2334-5664","authenticated-orcid":false,"given":"Peiguo","family":"Yang","sequence":"additional","affiliation":[{"name":"Westlake Laboratory of Life Sciences and Biomedicine School of Life Sciences Westlake University  Hangzhou Zhejiang 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