Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus

Matanic, Vanesa C Albiol; Castilla, Viviana

doi:10.1016/j.ijantimicag.2003.07.022

Cited by 172 publications

(105 citation statements)

References 25 publications

(39 reference statements)

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“…Antimicrobial peptides are produced by a variety of organisms including insects, fungi, Gram-positive and Gram-negative bacteria, and many of them have been reported as viral inhibitors [1, 28]. For example, cationic peptides like -defensins, hecate, and synthetic derivatives of magainins are active against HSV in vitro replication [6, 22] while melittin, a 26 amino acid amphipathic peptide isolated from the venom of the European honeybee Apis melliphera , inhibits the replication of both HIV and HSV [2, 6, 51]. Several antimicrobial peptides ribosomally produced by bacteria, collectively called bacteriocins, have been described for the members of the genus Enterococcus [7].…”

Section: Introductionmentioning

confidence: 99%

Safety, Formulation and In Vitro Antiviral Activity of the Antimicrobial Peptide Subtilosin Against Herpes Simplex Virus Type 1

Torres

Noll

et al. 2013

Probiotics & Antimicro. Prot.

104

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In the present study the antiviral properties of the bacteriocin subtilosin against Herpes simplex virus type 1 (HSV-1) and the safety and efficacy of a subtilosin-based nanofiber formulation were determined. High concentrations of subtilosin, the cyclical antimicrobial peptide produced by Bacillus amyloliquefaciens, were virucidal against HSV-1. Interestingly, at non-virucidal concentrations, subtilosin inhibited wild type HSV-1 and aciclovir-resistant mutants in a dose-dependent manner. Although the exact antiviral mechanism is not fully understood, time of addition experiments and western blot analysis suggest that subtilosin does not affect viral multiplication steps prior to protein synthesis. Poly(vinyl alcohol) (PVOH)-based subtilosin nanofibers with a width of 278 nm were produced by the electrospinning process. The retained antimicrobial activity of the subtilosin-based fibers was determined via an agar well diffusion assay. The loading capacity of the fibers was 2.4 mg subtilosin/g fiber, and loading efficiency was 31.6%. Furthermore, the nanofibers with and without incorporated subtilosin were shown to be nontoxic to human epidermal tissues using an in vitro human tissue model. Taking together these results subtilosin-based nanofibers should be further studied as a novel alternative method for treatment and/or control of HSV-1 infection.

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Section: Introductionmentioning

confidence: 99%

Safety, Formulation and In Vitro Antiviral Activity of the Antimicrobial Peptide Subtilosin Against Herpes Simplex Virus Type 1

Torres

Noll

et al. 2013

Probiotics & Antimicro. Prot.

104

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“…Indeed, it has been shown that some natural CPPs, which are rich in basic amino acids, exhibit different biologic activities, such as an antifungal or antimicrobial effect 37 . In addition, the antiviral activity of some CPPs has been reported toward enveloped viruses such as HSV and HIV38, 39, 40 and, more recently by us, for a CatLip displaying an inhibitory effect on hepadnaviral secretion 21, 41. However, the contribution of the antiviral activity of CPPs to the antisense potential of CPP-PNA conjugates was not explored.…”

Section: Discussionmentioning

confidence: 99%

Role of Cell-Penetrating Peptides in Intracellular Delivery of Peptide Nucleic Acids Targeting Hepadnaviral Replication

Ndeboko

Ramamurthy

Lémamy

et al. 2017

Molecular Therapy - Nucleic Acids

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Peptide nucleic acids (PNAs) are potentially attractive antisense agents against hepatitis B virus (HBV), although poor cellular uptake limits their therapeutic application. In the duck HBV (DHBV) model, we evaluated different cell-penetrating peptides (CPPs) for delivery to hepatocytes of a PNA-targeting hepadnaviral encapsidation signal (ε). This anti-ε PNA exhibited sequence-specific inhibition of DHBV RT in a cell-free system. Investigation of the best in vivo route of delivery of PNA conjugated to (D-Arg)8 (P1) showed that intraperitoneal injection to ducklings was ineffective, whereas intravenously (i.v.) injected fluorescein-P1-PNA reached the hepatocytes. Treatment of virus carriers with i.v.-administered P1-PNA resulted in a decrease in viral DNA compared to untreated controls. Surprisingly, a similar inhibition of viral replication was observed in vivo as well as in vitro in primary hepatocyte cultures for a control 2 nt mismatched PNA conjugated to P1. By contrast, the same PNA coupled to (D-Lys)4 (P2) inhibited DHBV replication in a sequence-specific manner. Interestingly, only P1, but not P2, displayed anti-DHBV activity in the absence of PNA cargo. Hence, we provide new evidence that CPP-PNA conjugates inhibit DHBV replication following low-dose administration. Importantly, our results demonstrate the key role of CPPs used as vehicles in antiviral specificity of CPP-PNA conjugates.

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“…Magainin-1 and -2 from X. laevis show antiviral properties against herpes simplex virus type 1 (HSV-1) and herpes simplex virus type 2 (HSV-2) but were inactive against the arenavirus, Junin virus The peptides do not appear to inactivate the HSV particles directly but rather target important steps in the viral reproductive cycle [74]. Magainin-2 and PGLa from X. laevis markedly reduced the infectivity of channel catfish virus but were less potent against frog virus 3 [75].…”

Section: Peptides With Anti-viral Activitymentioning

confidence: 99%

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

Conlon

Mechkarska

2014

Pharmaceuticals

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Skin secretions from frogs belonging to the genera Xenopus, Silurana, Hymenochirus, and Pseudhymenochirus in the family Pipidae are a rich source of host-defense peptides with varying degrees of antimicrobial activities and cytotoxicities to mammalian cells. Magainin, peptide glycine-leucine-amide (PGLa), caerulein-precursor fragment (CPF), and xenopsin-precursor fragment (XPF) peptides have been isolated from norepinephrine-stimulated skin secretions from several species of Xenopus and Silurana. Hymenochirins and pseudhymenochirins have been isolated from Hymenochirus boettgeri and Pseudhymenochirus merlini. A major obstacle to the development of these peptides as anti-infective agents is their hemolytic activities against human erythrocytes. Analogs of the magainins, CPF peptides and hymenochirin-1B with increased antimicrobial potencies and low cytotoxicities have been developed that are active (MIC < 5 μM) against multidrug-resistant clinical isolates of Staphylococcus aureus, Escherichia coli, Acinetobacter baumannii, Stenotrophomonas maltophilia and Klebsiella pneumoniae. Despite this, the therapeutic potential of frog skin peptides as anti-infective agents has not been realized so that alternative clinical applications as anti-cancer, anti-viral, anti-diabetic, or immunomodulatory drugs are being explored.

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Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus

Cited by 172 publications

References 25 publications

Safety, Formulation and In Vitro Antiviral Activity of the Antimicrobial Peptide Subtilosin Against Herpes Simplex Virus Type 1

Safety, Formulation and In Vitro Antiviral Activity of the Antimicrobial Peptide Subtilosin Against Herpes Simplex Virus Type 1

Role of Cell-Penetrating Peptides in Intracellular Delivery of Peptide Nucleic Acids Targeting Hepadnaviral Replication

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

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