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. 2024 Jun 12;16(6):948.
doi: 10.3390/v16060948.

Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1

Liana Costa Pereira Vilas Boas  1   2 , Danieli Fernanda Buccini  2   3 , Rhayfa Lorrayne Araújo Berlanda  1   2 , Bruno de Paula Oliveira Santos  4 , Mariana Rocha Maximiano  2   3 , Luciano Morais Lião  4 , Sónia Gonçalves  5 , Nuno C Santos  5 , Octávio Luiz Franco  1   2   3
Affiliations

Antiviral Activities of Mastoparan-L-Derived Peptides against Human Alphaherpesvirus 1

Liana Costa Pereira Vilas Boas et al. Viruses. .

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 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.

Keywords: antiviral peptide; mastoparan; peptide–membrane interaction.

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Conflict of interest statement

The authors declare no conflicts of interest. All authors contributed to the study design, data analysis or interpretation, and to revising the manuscript. Liana Costa Pereira Vilas Boas performed material preparation and data collection.

Figures

Figure 1
Figure 1
In vitro assays of the antiviral activity of the peptides mastoparan-MO, mastoparan-L, and [I5, R8] mastoparan. (A) Heat map showing MTT cell culture viability assays with the three mastoparans. (B) Antiviral triage assay with the three peptides. (C) Dose–response curves of the peptides mastoparan MO and [I5, R8] mastoparan. Acyclovir (ACV) was used as a positive control for inhibition (D) Time-addition assay of the peptides mastoparan MO and [I5, R8] mastoparan. The positive-negative control with only the cells infected with the HSV-1 was marked as not treated. * NT—Not treated.
Figure 2
Figure 2
Tridimensional structure of [I5, R8] mastoparan obtained by NMR. (A,B) Analysis of the connectivity pattern for [I5, R8] mastoparan. (C) Overlapping of the ten structures with less energy and cloud model structure.
Figure 3
Figure 3
Interaction of the peptide [I5, R8] mastoparan with lipid vesicles labeled with TMA-DPH (A) and DPH (B), followed by fluorescence anisotropy measurements.
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References

    1. Rechenchoski D.Z., Faccin-Galhardi L.C., Linhares R.E.C., Nozawa C. Herpesvirus: An Underestimated Virus. Folia Microbiol. 2017;62:151–156. doi: 10.1007/s12223-016-0482-7. - DOI - PubMed
    1. Roizman B., Whitley R.J. An Inquiry into the Molecular Basis of HSV Latency and Reactivation. Annu. Rev. Microbiol. 2013;67:355–374. doi: 10.1146/annurev-micro-092412-155654. - DOI - PubMed
    1. Matthias J., Du Bernard S., Schillinger J.A., Hong J., Pearson V., Peterman T.A. Estimating Neonatal Herpes Simplex Virus Incidence and Mortality Using Capture-Recapture, Florida. Clin. Infect. Dis. 2021;73:506–512. doi: 10.1093/cid/ciaa727. - DOI - PMC - PubMed
    1. Looker K.J., Magaret A.S., May M.T., Turner K.M.E., Vickerman P., Gottlieb S.L., Newman L.M. Global and Regional Estimates of Prevalent and Incident Herpes Simplex Virus Type 1 Infections in 2012. PLoS ONE. 2015;10:e0140765. doi: 10.1371/journal.pone.0140765. - DOI - PMC - PubMed
    1. James C., Harfouche M., Welton N.J., Turner K.M.E., Abu-Raddad L.J., Gottlieb S.L., Looker K.J. Herpes Simplex Virus: Global Infection Prevalence and Incidence Estimates, 2016. Bull. World Health Organ. 2020;98:315–329. doi: 10.2471/BLT.19.237149. - DOI - PMC - PubMed

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