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Glycyrrhizic Acid Inhibits SARS-CoV-2 Infection by Blocking Spike Protein-Mediated Cell Attachment.
Li, Jingjing; Xu, Dongge; Wang, Lingling; Zhang, Mengyu; Zhang, Guohai; Li, Erguang; He, Susu.
  • Li J; State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Nanjing 210093, China.
  • Xu D; Jiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing University, Nanjing 210093, China.
  • Wang L; Jiangsu Topcel Biological Technology Co., Ltd., Nanjing 210093, China.
  • Zhang M; State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Nanjing 210093, China.
  • Zhang G; Jiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing University, Nanjing 210093, China.
  • Li E; Yancheng Medical Research Centre, Medical School, Nanjing University, Yancheng 224000, China.
  • He S; State Key Laboratory of Pharmaceutical Biotechnology, Medical School, Nanjing University, Nanjing 210093, China.
Molecules ; 26(20)2021 Oct 09.
Article in English | MEDLINE | ID: covidwho-1463773
ABSTRACT
Glycyrrhizic acid (GA), also known as glycyrrhizin, is a triterpene glycoside isolated from plants of Glycyrrhiza species (licorice). GA possesses a wide range of pharmacological and antiviral activities against enveloped viruses including severe acute respiratory syndrome (SARS) virus. Since the S protein (S) mediates SARS coronavirus 2 (SARS-CoV-2) cell attachment and cell entry, we assayed the GA effect on SARS-CoV-2 infection using an S protein-pseudotyped lentivirus (Lenti-S). GA treatment dose-dependently blocked Lenti-S infection. We showed that incubation of Lenti-S virus, but not the host cells with GA prior to the infection, reduced Lenti-S infection, indicating that GA targeted the virus for infection. Surface plasmon resonance measurement showed that GA interacted with a recombinant S protein and blocked S protein binding to host cells. Autodocking analysis revealed that the S protein has several GA-binding pockets including one at the interaction interface to the receptor angiotensin-converting enzyme 2 (ACE2) and another at the inner side of the receptor-binding domain (RBD) which might impact the close-to-open conformation change of the S protein required for ACE2 interaction. In addition to identifying GA antiviral activity against SARS-CoV-2, the study linked GA antiviral activity to its effect on virus cell binding.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Glycyrrhizic Acid / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Limits: Humans Language: English Journal subject: Biology Year: 2021 Document Type: Article Affiliation country: Molecules26206090

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Glycyrrhizic Acid / Spike Glycoprotein, Coronavirus / SARS-CoV-2 Limits: Humans Language: English Journal subject: Biology Year: 2021 Document Type: Article Affiliation country: Molecules26206090