Antiviral Peptide

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Viral Immunology, Vaccines, and Antivirals".

Deadline for manuscript submissions: closed (1 March 2024) | Viewed by 4487

Special Issue Editors


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Guest Editor
Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China
Interests: antiviral; peptide; coronavirus; HIV; fusion inhibitor; six-helix boundle; cell-cell fusion

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Guest Editor
Department of Microbiology, School of Clinical Medicine, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong, China
Interests: antiviral; board spectrum; branched peptide; defensin; fusion inhibitor; respiratroy viruses; viral release; viral transmission

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Guest Editor
State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, China
Interests: antiviral agent; peptide; HIV; coronavirus; broad spectrum; entry inhibitor

Special Issue Information

Deal Colleagues,

Twenty years ago, the first anti-HIV peptide drug, enfuvirtide (also known as T20), was approved by the US FDA for the clinical treatment of HIV infection, thus opening up a new avenue for the development of antiviral peptide drugs. Since then, numerous antiviral peptides have been reported to be effective against various viruses including severe acute respiratory syndrome coronavirus (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Ebola virus (EBOV), Hendra virus (HeV), Nipah virus (NiV), influenza virus (IFV), parainfluenza virus (PIV), Zika virus (ZIKV), Dengue virus (DENV), hepatitis C virus (HCV), and hepatitis B virus (HBV).  Representative antiviral peptides, such as boceprevir against HBV and hepatitis D virus, telaprevir against HCV, and the pan-CoV fusion inhibitor peptide EK1, are now in clinical uses or clinical trials and show advantages including broad-spectrum antiviral activities, low metabolic toxicity, and a high barrier to viral drug resistance. Peptides offer the potential to fill the gap between conventional small-molecule drugs and protein-based drugs and represent a class of molecules that have the specificity and potency of protein biologics but are very amenable to site-specific modification to create new lead compounds. In recent years, much progress has been made regarding the development of medicinal chemistry strategies, contributing to the discovery of new peptide-based drugs that work against current and future threats due to emerging and re-emerging viral pandemics. Therefore, antiviral peptides have become an important component of antivirals and hold great promise for combating chronic and acute viral infections.

For this Special Issue, both research and review articles are welcome. Topics include, but are not limited to, the following research areas:

  1. The development of antiviral peptides or peptidomimetics targeting virus or host for the treatment or prevention of viral infection;
  2. In vitro or in vivo evaluation of antiviral peptides or peptidomimetics;
  3. Preclinical or clinical studies of antiviral peptides;
  4. The application of artificial intelligence for the discovery or optimization of antiviral peptides;
  5. Novel medicinal chemistry strategies and drug targets in antiviral peptide discovery.

Dr. Shuai Xia
Dr. Hanjun Zhao
Dr. Chao Wang
Guest Editors

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Keywords

  • antiviral agent
  • coronavirus
  • defensin
  • enveloped viruses
  • entry inhibitor
  • fusion inhibitor
  • HIV
  • peptide
  • respiratory viruses
  • drug design
  • novel target
  • medicinal chemistry strategies

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Published Papers (2 papers)

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Research

22 pages, 6177 KiB  
Article
The Virus Entry Pathway Determines Sensitivity to the Antiviral Peptide TAT-I24
by Eva Kicker, Antonio Kouros, Kurt Zatloukal and Hanna Harant
Viruses 2025, 17(4), 458; https://doi.org/10.3390/v17040458 - 23 Mar 2025
Viewed by 2581
Abstract
The peptide TAT-I24, a fusion of the TAT peptide (amino acids 48–60) and the 9-mer peptide I24, has been previously shown to neutralize several double-stranded (ds) DNA viruses in vitro. We have now extended the testing to potentially sensitive RNA viruses and analyzed [...] Read more.
The peptide TAT-I24, a fusion of the TAT peptide (amino acids 48–60) and the 9-mer peptide I24, has been previously shown to neutralize several double-stranded (ds) DNA viruses in vitro. We have now extended the testing to potentially sensitive RNA viruses and analyzed the antiviral effect of the peptide against Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). In Vero E6 cells, TAT-I24 neutralized the human 2019-nCoV isolate (Wuhan variant) in a dose-dependent manner, while it was unable to neutralize two SARS-CoV-2 variants of concern, Delta and Omicron. Moreover, TAT-I24 could not significantly neutralize any of the SARS-CoV-2 variants in the human lung carcinoma cell line Calu-3, which provides an alternative entry route for SARS-CoV-2 by direct membrane fusion. Therefore, a possible dependence on virus uptake by endocytosis was investigated by exposing Vero E6 cells to chloroquine (CQ), an inhibitor of endosomal acidification. The Wuhan variant was highly sensitive to inhibition by CQ, an effect which was further enhanced by TAT-I24, while the Delta variant was less sensitive to inhibition by higher concentrations of CQ compared to the Wuhan variant. The microscopic analysis of COS-7 cells using a rhodamine-labeled TAT-I24 (Rho-TAT-I24) showed the endosomal localization of fluorescent TAT-I24 and co-localization with transfected GFP-Rab14 but not GFP-Rab5. As these proteins are found in distinct endosomal pathways, our results indicate that the virus entry pathway determines sensitivity to the peptide. Full article
(This article belongs to the Special Issue Antiviral Peptide)
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13 pages, 1215 KiB  
Article
Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1
by Liana Costa Pereira Vilas Boas, Danieli Fernanda Buccini, Rhayfa Lorrayne Araújo Berlanda, Bruno de Paula Oliveira Santos, Mariana Rocha Maximiano, Luciano Morais Lião, Sónia Gonçalves, Nuno C. Santos and Octávio Luiz Franco
Viruses 2024, 16(6), 948; https://doi.org/10.3390/v16060948 - 12 Jun 2024
Cited by 2 | Viewed by 1345
Abstract
Human alphaherpesvirus 1 (HSV-1) is a significantly widespread viral pathogen causing recurrent infections that are currently incurable despite available treatment protocols. Studies have highlighted the potential of antimicrobial peptides sourced from Vespula lewisii venom, particularly those belonging to the mastoparan family, as effective [...] Read more.
Human alphaherpesvirus 1 (HSV-1) is a significantly widespread viral pathogen causing recurrent infections that are currently incurable despite available treatment protocols. Studies have highlighted the potential of antimicrobial peptides sourced from Vespula lewisii venom, particularly those belonging to the mastoparan family, as effective against HSV-1. This study aimed to demonstrate the antiviral properties of mastoparans, including mastoparan-L [I5, R8], mastoparan-MO, and [I5, R8] mastoparan, against HSV-1. Initially, Vero cell viability was assessed in the presence of these peptides, followed by the determination of antiviral activity, mechanism of action, and dose-response curves through plaque assays. Structural analyses via circular dichroism and nuclear magnetic resonance were conducted, along with evaluating membrane fluidity changes induced by [I5, R8] mastoparan using fluorescence-labeled lipid vesicles. Cytotoxic assays revealed high cell viability (>80%) at concentrations of 200 µg/mL for mastoparan-L and mastoparan-MO and 50 µg/mL for [I5, R8] mastoparan. Mastoparan-MO and [I5, R8] mastoparan exhibited over 80% HSV-1 inhibition, with up to 99% viral replication inhibition, particularly in the early infection stages. Structural analysis indicated an α-helical structure for [I5, R8] mastoparan, suggesting effective viral particle disruption before cell attachment. Mastoparans present promising prospects for HSV-1 infection control, although further investigation into their mechanisms is warranted. Full article
(This article belongs to the Special Issue Antiviral Peptide)
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