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Cathelicidin-derived antiviral peptide inhibits herpes simplex virus 1 infection.

Authors :
Guo X
An Y
Tan W
Ma L
Wang M
Li J
Li B
Hou W
Wu L
Source :
Frontiers in microbiology [Front Microbiol] 2023 Jun 05; Vol. 14, pp. 1201505. Date of Electronic Publication: 2023 Jun 05 (Print Publication: 2023).
Publication Year :
2023

Abstract

Herpes simplex virus 1 (HSV-1) is a widely distributed virus. HSV-1 is a growing public health concern due to the emergence of drug-resistant strains and the current lack of a clinically specific drug for treatment. In recent years, increasing attention has been paid to the development of peptide antivirals. Natural host-defense peptides which have uniquely evolved to protect the host have been reported to have antiviral properties. Cathelicidins are a family of multi-functional antimicrobial peptides found in almost all vertebrate species and play a vital role in the immune system. In this study, we demonstrated the anti-HSV-1 effect of an antiviral peptide named WL-1 derived from human cathelicidin. We found that WL-1 inhibited HSV-1 infection in epithelial and neuronal cells. Furthermore, the administration of WL-1 improved the survival rate and reduced viral load and inflammation during HSV-1 infection via ocular scarification. Moreover, facial nerve dysfunction, involving the abnormal blink reflex, nose position, and vibrissae movement, and pathological injury were prevented when HSV-1 ear inoculation-infected mice were treated with WL-1. Together, our findings demonstrate that WL-1 may be a potential novel antiviral agent against HSV-1 infection-induced facial palsy.<br />Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.<br /> (Copyright © 2023 Guo, An, Tan, Ma, Wang, Li, Li, Hou and Wu.)

Details

Language :
English
ISSN :
1664-302X
Volume :
14
Database :
MEDLINE
Journal :
Frontiers in microbiology
Publication Type :
Academic Journal
Accession number :
37342565
Full Text :
https://doi.org/10.3389/fmicb.2023.1201505