ArticleAntimicrobial agents and chemotherapy2007
Addition of a C-terminal cysteine improves the anti-herpes simplex virus activity of a peptide containing the human immunodeficiency virus type 1 TAT protein transduction domain.
Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Identification of Novel TAT-I24-Related Peptides with Antiviral Activities.International journal of molecular sciences · 2025Article
- Article
- In Vitro Profiling of the Antiviral Peptide TAT-I24.International journal of molecular sciences · 2024Article
- Pathobiology and treatment of viral keratitis.Experimental eye research · 2021Review
- A Novel, Broad-Acting Peptide Inhibitor of Double-Stranded DNA Virus Gene Expression and Replication.Frontiers in microbiology · 2020Article
- Current and Emerging Therapies for Ocular Herpes Simplex Virus Type-1 Infections.Microorganisms · 2019Review
- Epimerization-free access to C-terminal cysteine peptide acids, carboxamides, secondary amides, and estersChemical science · 2018Article
- Extended Release of an Anti-Heparan Sulfate Peptide From a Contact Lens Suppresses Corneal Herpes Simplex Virus-1 Infection.Investigative ophthalmology & visual science · 2016Article
- Peptide therapeutics for treating ocular surface infections.Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics · 2014Review
- A cationic peptide, TAT-Cd°, inhibits herpes simplex virus type 1 ocular infection in vivo.Investigative ophthalmology & visual science · 2013Article
- Ocular herpes simplex virus: how are latency, reactivation, recurrent disease and therapy interrelated?Future microbiology · 2011Review
- A cationic TAT peptide inhibits Herpes simplex virus type 1 infection of human corneal epithelial cells.Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics · 2010Article
- The virucidal EB peptide protects host cells from herpes simplex virus type 1 infection in the presence of serum albumin and aggregates proteins in a detergent-like manner.Antimicrobial agents and chemotherapy · 2010Article
- Cell-Penetrating Peptides for Antiviral Drug Development.Pharmaceuticals (Basel, Switzerland) · 2010Review
- Article
- Characterization of a peptide domain within the GB virus C NS5A phosphoprotein that inhibits HIV replication.PloS one · 2008Article
- Inhibition of herpes simplex virus type 1 infection by cationic beta-peptides.Antimicrobial agents and chemotherapy · 2008Article
- Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cells.Journal of virology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Previous studies have shown that peptides containing the protein transduction domain (PTD) of the human immunodeficiency virus tat protein (GRKKRRQRRR) were effective inhibitors of herpes simplex virus type 1 (HSV-1) entry (H. Bultmann and C. R. Brandt, J. Biol. Chem. 277:36018-36023, 2002). We now show that the addition of a single cysteine residue to the C terminus of the TAT PTD (TAT-C peptide) improves the antiviral activity against HSV-1 and HSV-2. The principle effect of adding the cysteine was to enable the peptide to inactivate virions and to induce a state of resistance to infection in cells pretreated with peptide. The TAT-C peptide acted extracellularly, immediately blocked entry of adsorbed virus, prevented VP16 translocation to the nucleus, and blocked syncytium formation and cell-cell spread. Thus, TAT-C peptides are fusion inhibitors. The induction of the resistance of cells to infection was rapid, recovered with a half-life of 5 to 6 h, and could be reinduced by peptide treatment. TAT-C bound to heparan sulfate but was a poor competitor for viral attachment. The antiviral activity depended on the net positive charge of the peptide but not on chirality, and a free sulfhydryl group was not essential for antiviral activity because TAT-C dimers were at least as effective as monomers. The unique combination of antiviral activities and low toxicity combine to make TAT-C a strong candidate for further development as a drug to block HSV infection.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.