Emodin blocks the SARS coronavirus spike protein and angiotensin-converting enzyme 2 interaction

• Published in: Antiviral research 2007-05, Vol.74 (2), p.92-101
• Main Authors: Ho, Tin-Yun, Wu, Shih-Lu, Chen, Jaw-Chyun, Li, Chia-Cheng, Hsiang, Chien-Yun
• Format: Article
• Language: English
• Subjects: Angiotensin-Converting Enzyme 2; Angiotensin-Converting Enzyme Inhibitors - pharmacology; Animals; Antibiotics. Antiinfectious agents. Antiparasitic agents; Antiviral agents; Antiviral Agents - pharmacology; Biological and medical sciences; Chlorocebus aethiops; Coronavirus - drug effects; Dose-Response Relationship, Drug; Drugs, Chinese Herbal - pharmacology; Emodin; Emodin - isolation & purification; Emodin - pharmacology; Medical sciences; Membrane Glycoproteins - metabolism; Peptidyl-Dipeptidase A - metabolism; Pharmacology. Drug treatments; Plants, Medicinal - chemistry; Polygonaceae; Polygonum - chemistry; Polygonum multiflorum; Retroviridae - drug effects; Rheum; Rheum - chemistry; SARS coronavirus; SARS Virus - drug effects; SARS Virus - metabolism; Spike Glycoprotein, Coronavirus; Spike protein; Vero Cells; Viral Envelope Proteins - metabolism
• ISSN: 0166-3542; 1872-9096
• DOI: 10.1016/j.antiviral.2006.04.014

Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). SARS-CoV spike (S) protein, a type I membrane-bound protein, is essential for the viral attachment to the host cell receptor angiotensin-converting enzyme 2 (ACE2). By screening 312 controlled Chinese medicinal herbs supervised by Committee on Chinese Medicine and Pharmacy at Taiwan, we identified that three widely used Chinese medicinal herbs of the family Polygonaceae inhibited the interaction of SARS-CoV S protein and ACE2. The IC 50 values for Radix et Rhizoma Rhei (the root tubers of Rheum officinale Baill.), Radix Polygoni multiflori (the root tubers of Polygonum multiflorum Thunb.), and Caulis Polygoni multiflori (the vines of P. multiflorum Thunb.) ranged from 1 to 10 μg/ml. Emodin, an anthraquinone compound derived from genus Rheum and Polygonum, significantly blocked the S protein and ACE2 interaction in a dose-dependent manner. It also inhibited the infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. These findings suggested that emodin may be considered as a potential lead therapeutic agent in the treatment of SARS.