Rosmarinic acid inhibits Rift Valley fever virus: in vitro, computational and analytical studies.

Autor: Farouk, Faten, Zarka, Mohamed A, Al-Sawahli, Majid Mohammed, Hassan, Amr, Mohamed, Aly Fahmy, Ibrahim, Ibrahim M, El-Rahman Mohammed, Fafy Abd, Shebl, Rania Ibrahim
Zdroj: Future Virology; Oct2023, Vol. 18 Issue 15, p1001-1019, 19p
Abstrakt: Aim: The antiviral potentials of rosmarinic acid (RA) against Rift Valley fever (RVF) virus were investigated. Methods: Antiviral activity was investigated by evaluating the reduction in the viral infectivity titer. Computational and LC–MS studies were performed for investigating the mechanism of action. This is via testing the interaction between RA and its major metabolite with the key infectivity proteins and determination of RA cellular permeability. Results: A superior reduction in RVF infectivity titer (45.5%) was observed when RA was applied post-infection compared to 17.7% reduction following its application before infection in addition to time-dependent inactivation kinetics. Recorded data showed in-silico inhibitory potential of RA and its metabolite against RVFV cap-binding protein and glycoprotein C, which are integral for viral transcription. LC–MS revealed cellular inclusion of RA, supporting its intracellular viral interaction. Conclusion: These antiviral potentials might suggest a promising foundation for future anti-RVF drug development. Rift Valley fever virus is a virus that causes disease in animals and humans. This study looked at the ability of rosmarinic acid to stop the virus. Rosmarinic acid helped the cells that were affected by the virus, but it mildly protected the healthy cells. Our computer models showed that rosmarinic acid acts on the virus more than its effect on the cells. These results might show potential for the development of new drugs to tackle this virus. Rosmarinic acid (RA) exhibits promising antiviral potential against RVFV. In-silico studies show its strong binding affinity to the RVFV cap-binding protein, which is engaged in the viral transcription and interaction with glycoprotein C, which is important for cellular entry. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index