Repurposing Vancomycin as a Potential Antiviral Agent Against PEDV via nsp13 Helicase Inhibition
by
Qiao Chen
1,2, 
Mengqi Yu
1,2,
Jiajing Guo
1,2,
Jingqi Qiu
1,2,
Fei Liu
1,2,* and
Yanke Shan
1,2,* 1
Joint International Research Laboratory of Animal Health and Food Safety of Ministry of Education, Nanjing Agricultural University, Nanjing 210095, China
2
Single Molecule Biochemistry & Biomedicine Laboratory (Sinmolab), Nanjing Agricultural University, Nanjing 210095, China
*
Authors to whom correspondence should be addressed.
Animals 2025, 15(7), 923; https://doi.org/10.3390/ani15070923
Submission received: 6 February 2025
/
Revised: 19 March 2025
/
Accepted: 20 March 2025
/
Published: 23 March 2025
(This article belongs to the Section Veterinary Clinical Studies)
Simple Summary
Porcine epidemic diarrhea virus (PEDV) is an extremely virulent coronavirus in the swine industry, causing severe economic losses globally. Given the lack of effective antiviral therapies, this study identified that Vancomycin, a glycopeptide antibiotic, effectively inhibits both the NTPase and RNA helicase activities of PEDV non-structural protein 13 (nsp13) in a dose-dependent manner, resulting in highly effective reduced viral replication in vitro. These findings highlight the potential of Vancomycin as a candidate for antiviral drug repurposing against PEDV, offering a promising approach for controlling PEDV outbreaks.
Abstract
Porcine epidemic diarrhea virus (PEDV) causes a highly contagious intestinal disease with severe economic impacts on the global swine industry. The non-structural protein 13 (nsp13), a viral helicase, is essential for viral replication, making it a promising target for antiviral drug development. In this study, through virtual screening and molecular dynamics simulations, Vancomycin, a small-molecule drug also clinically used as an antibacterial agent, was identified to exhibit a stable binding affinity for PEDV nsp13. The NTPase and ATP-dependent RNA helicase activities of PEDV nsp13 were confirmed in vitro, and the optimal biochemical reaction conditions for its dsRNA unwinding activity were established. Further experiments demonstrated that Vancomycin effectively inhibited the dual enzymatic activities of PEDV nsp13 and reduced PEDV infections in vitro. This research highlights Vancomycin as a novel inhibitor of PEDV nsp13, providing valuable mechanistic insights and serving as a model for antiviral drug discovery. While this study suggests its potential for repurposing as a therapeutic agent against PEDV, further investigations are required to evaluate its feasibility in vivo, particularly in terms of safety, efficacy, and practical applicability.
