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Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease.
Liu, Jiankai; Kan, Mujie; Zhang, Lianzhi; Yue, Yuan; Wang, Shaohua; Hong, Min; Hong, Xinyu.
  • Liu J; Biochemistry Department, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
  • Kan M; Biochemistry Department, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
  • Zhang L; Biochemistry Department, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
  • Yue Y; Laboratory of Medical Biology Center, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
  • Wang S; Institute of Virology and AIDS Research, The First Hospital of Jilin University, Changchun 130021, China.
  • Hong M; Biochemistry Department, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
  • Hong X; Neuroscience Research Laboratory, Neurosurgery Department, The First Hospital of Jilin University, Jilin University, Changchun 130021, China.
Molecules ; 27(6)2022 Mar 14.
Article in English | MEDLINE | ID: covidwho-1742557
ABSTRACT
The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV-2 virus, especially the S1 subunit, is very sensitive to alkaline serine protease with acidic pI (ASPNJ), NJ represents Neanthes japonica (Izuka) from which ASP is purified). ASPNJ cleaves proteins when the carbonyl group of the peptide bond is contributed by arginine or lysine. ASPNJ can degrade the S protein very quickly and effectively in vitro with relative selectivity. It can be inferred that the S, S1 and RBD of SARS-CoV-2 variants can also be easily degraded by ASPNJ. This rapid and strong degradation of the S protein by ASPNJ may become a potential new treatment strategy.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Serine Proteases / COVID-19 Topics: Variants Limits: Humans Language: English Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Molecules27061882

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Serine Proteases / COVID-19 Topics: Variants Limits: Humans Language: English Journal subject: Biology Year: 2022 Document Type: Article Affiliation country: Molecules27061882