Your browser doesn't support javascript.
loading
Emodin inhibits respiratory syncytial virus entry by interactions with fusion protein.
Xiong, Yingcai; Tan, Guangxing; Tao, Keyu; Zhou, Yinghui; Li, Jun; Ou, Weiying; Shen, Cunsi; Xie, Tong; Zhang, Chao; Hou, Yayi; Ji, Jianjian.
Afiliación
  • Xiong Y; Wuxi Traditional Chinese Medicine Hospial Afiliated to Nanjing University of Chinese Medicine, Wuxi 214071, China.
  • Tan G; School of Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
  • Tao K; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
  • Zhou Y; Wuxi Traditional Chinese Medicine Hospial Afiliated to Nanjing University of Chinese Medicine, Wuxi 214071, China.
  • Li J; School of Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
  • Ou W; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
  • Shen C; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
  • Xie T; School of Medicine, Nanjing University of Chinese Medicine, Nanjing, China.
  • Zhang C; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
  • Hou Y; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
  • Ji J; Jiangsu Key Laboratory of Pediatric Respiratory Disease, Institute of Pediatrics, Nanjing University of Chinese Medicine, Nanjing, China.
Front Microbiol ; 15: 1393511, 2024.
Article en En | MEDLINE | ID: mdl-38817970
ABSTRACT

Introduction:

Respiratory syncytial virus (RSV) fusion (F) protein is essential for facilitating virus entry into host cells, providing a hopeful path for combating viral diseases. However, F protein inhibitors can rapidly select for viral resistance. Thus, discovering new inhibitors of F-protein is necessary to enrich the RSV drug development pipeline.

Methods:

In this study, we screen 25 bioactive compounds from Chinese herbal medicines that exhibit a strong binding to the RSV-F protein using surface plasmon resonance.

Results:

After screening, we found emodin could strongly bind to RSV-F protein, and could effectively curb RSV infection. Further investigations certificated that emodin specifically disrupts the attachment and internalization phases of RSV infection by targeting the RSV-F protein. In vivo studies with mice infected with RSV demonstrated that emodin effectively reduces lung pathology. This therapeutic effect is attributed to emodin's capacity to diminish pro-inflammatory cytokine production and reduce viral load in the lungs.

Discussion:

In conclusion, our findings provide initial insights into the mechanism by which emodin counters RSV infection via engagement with the RSV-F protein, establishing it as a viable contender for the development of novel therapeutic agents aimed at RSV.
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Microbiol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Microbiol Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza