ArticleThe Journal of biological chemistry2010
The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Article
- Screening and Identification of Multiple Peptides Homologous to the Fusion Glycoprotein Gc of Schmallenberg Virus Able to Inhibit Viral Infection.Transboundary and emerging diseases · 2025Article
- Peptide-based delivery of therapeutics in cancer treatment.Materials today. Bio · 2022Review
- Association Mechanism of Peptide-Coated Metal Nanoparticles with Model Membranes: A Coarse-Grained Study.Journal of chemical theory and computation · 2021Article
- Peptides and Dendrimers: How to Combat Viral and Bacterial Infections.Pharmaceutics · 2021Review
- Eradication of Candida albicans persister cell biofilm by the membranotropic peptide gH625.Scientific reports · 2020Article
- Quantum dots functionalized with gH625 attenuate QDs oxidative stress and lethality in Caenorhabditis elegans: a model system.Ecotoxicology (London, England) · 2020Article
- Enhanced uptake of gH625 by blood brain barrier compared to liver in vivo: characterization of the mechanism by an in vitro model and implications for delivery.Scientific reports · 2018Article
- Comparison Between Folic Acid and gH625 Peptide-Based Functionalization of FeNanoscale research letters · 2018Article
- Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625.Scientific reports · 2017Article
- Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Antimicrobial Dendrimeric Peptides: Structure, Activity and New Therapeutic Applications.International journal of molecular sciences · 2017Review
- Article
- Liposome armed with herpes virus-derived gH625 peptide to overcome doxorubicin resistance in lung adenocarcinoma cell lines.Oncotarget · 2016Article
- Membranotropic Cell Penetrating Peptides: The Outstanding Journey.International journal of molecular sciences · 2015Review
- gH625: a milestone in understanding the many roles of membranotropic peptides.Biochimica et biophysica acta · 2015Review
- Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood-brain barrier in rats.International journal of nanomedicine · 2015Article
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
- Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules.Journal of the Royal Society, Interface · 2014Review
- Exploitation of viral properties for intracellular delivery.Journal of peptide science : an official publication of the European Peptide Society · 2014Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpes simplex virus type 1 (HSV-1)-induced membrane fusion remains one of the most elusive mechanisms to be deciphered in viral entry. The structure resolution of glycoprotein gB has revealed the presence of fusogenic domains in this protein and pointed out the key role of gB in the entry mechanism of HSV-1. A second putative fusogenic glycoprotein is represented by the heterodimer comprising the membrane-anchored glycoprotein H (gH) and the small secreted glycoprotein L, which remains on the viral envelope in virtue of its non-covalent interaction with gH. Different domains scattered on the ectodomain of HSV-1 gH have been demonstrated to display membranotropic characteristics. The segment from amino acid 626 to 644 represents the most fusogenic region identified by studies with synthetic peptides and model membranes. Herein we have identified the minimal fusogenic sequence present on gH. An enlongation at the N terminus of a single histidine (His) has proved to profoundly increase the fusogenic activity of the original sequence. Nuclear magnetic resonance (NMR) studies have shown that the addition of the N-terminal His contributes to the formation and stabilization of an alpha-helical domain with high fusion propensity.
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