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SARS-CoV-2 impairs the disassembly of stress granules and promotes ALS-associated amyloid aggregation.
Li, Yichen; Lu, Shuaiyao; Gu, Jinge; Xia, Wencheng; Zhang, Shengnan; Zhang, Shenqing; Wang, Yan; Zhang, Chong; Sun, Yunpeng; Lei, Jian; Liu, Cong; Su, Zhaoming; Yang, Juntao; Peng, Xiaozhong; Li, Dan.
  • Li Y; Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China.
  • Lu S; School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200030, China.
  • Gu J; National Kunming High-level Biosafety Primate Research Center, Institute of Medical Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Kunming, 650031, China.
  • Xia W; State Key Laboratory of Medical Molecular Biology, Chinese Academy of Medical Sciences, School of Basic Medicine, Peking Union Medical College, Beijing, 100005, China.
  • Zhang S; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.
  • Zhang S; University of Chinese Academy of Sciences, Beijing, 100049, China.
  • Wang Y; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.
  • Zhang C; University of Chinese Academy of Sciences, Beijing, 100049, China.
  • Sun Y; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.
  • Lei J; University of Chinese Academy of Sciences, Beijing, 100049, China.
  • Liu C; Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China.
  • Su Z; School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200030, China.
  • Yang J; State Key Laboratory of Biotherapy, Department of Geriatrics and National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, Chengdu, 610041, China.
  • Peng X; State Key Laboratory of Biotherapy, Department of Geriatrics and National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, Chengdu, 610041, China.
  • Li D; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China.
Protein Cell ; 13(8): 602-614, 2022 08.
Article in English | MEDLINE | ID: covidwho-1777862
ABSTRACT
The nucleocapsid (N) protein of SARS-CoV-2 has been reported to have a high ability of liquid-liquid phase separation, which enables its incorporation into stress granules (SGs) of host cells. However, whether SG invasion by N protein occurs in the scenario of SARS-CoV-2 infection is unknow, neither do we know its consequence. Here, we used SARS-CoV-2 to infect mammalian cells and observed the incorporation of N protein into SGs, which resulted in markedly impaired self-disassembly but stimulated cell cellular clearance of SGs. NMR experiments further showed that N protein binds to the SG-related amyloid proteins via non-specific transient interactions, which not only expedites the phase transition of these proteins to aberrant amyloid aggregation in vitro, but also promotes the aggregation of FUS with ALS-associated P525L mutation in cells. In addition, we found that ACE2 is not necessary for the infection of SARS-CoV-2 to mammalian cells. Our work indicates that SARS-CoV-2 infection can impair the disassembly of host SGs and promote the aggregation of SG-related amyloid proteins, which may lead to an increased risk of neurodegeneration.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: COVID-19 / Amyotrophic Lateral Sclerosis Type of study: Risk factors Limits: Animals Language: English Journal: Protein Cell Journal subject: Biochemistry Year: 2022 Document Type: Article Affiliation country: S13238-022-00905-7

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Full text: Available Collection: International databases Database: MEDLINE Main subject: COVID-19 / Amyotrophic Lateral Sclerosis Type of study: Risk factors Limits: Animals Language: English Journal: Protein Cell Journal subject: Biochemistry Year: 2022 Document Type: Article Affiliation country: S13238-022-00905-7