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 (481 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2010 May 28; 285(22): 17123-17136.
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Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952758845&partnerID=40&md5=ca6d9ec1c38ab3d8e6377c48f09ec5ce
Keywords: Different Domains, Ectodomain, Helical Domains, Herpes Simplex Virus Type 1, Heterodimers, Histidine Residues, Membrane Fusion, Model Membranes, N-Terminals, Non-Covalent Interaction, Synthetic Peptide, Amino Acids, Cell Membranes, Magnetic Domains, Nuclear Magnetic Resonance, Organic Acids, Phosphatases, Glycoproteins, Unclassified Drug, Virus Glycoprotein, Alpha Helix, Amino Terminal Sequence, Article, Controlled Study, Nonhuman, Priority Journal, Protein Domain, Acrylamide, Algorithms, Herpesvirus 1, Kinetics, Lipids, Liposomes, Magnetic Resonance Spectroscopy, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Surface Plasmon Resonance, Tryptophan, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy. sgaldier@unina.it
Dept. of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy
Dept. of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, Napoli 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli 80134, Italy
Istituto di Biostrutture e Bioimmagini-Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, Napoli 80134, Italy
Department of Environmental Sciences, II University of Naples, via Vivaldi 43, Caserta 81100, Italy
References:
Not available.
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2010 May 28; 285(22): 17123-17136.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952758845&partnerID=40&md5=ca6d9ec1c38ab3d8e6377c48f09ec5ce
Keywords: Different Domains, Ectodomain, Helical Domains, Herpes Simplex Virus Type 1, Heterodimers, Histidine Residues, Membrane Fusion, Model Membranes, N-Terminals, Non-Covalent Interaction, Synthetic Peptide, Amino Acids, Cell Membranes, Magnetic Domains, Nuclear Magnetic Resonance, Organic Acids, Phosphatases, Glycoproteins, Unclassified Drug, Virus Glycoprotein, Alpha Helix, Amino Terminal Sequence, Article, Controlled Study, Nonhuman, Priority Journal, Protein Domain, Acrylamide, Algorithms, Herpesvirus 1, Kinetics, Lipids, Liposomes, Magnetic Resonance Spectroscopy, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Surface Plasmon Resonance, Tryptophan, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy. sgaldier@unina.it
Dept. of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy
Dept. of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, Napoli 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli 80134, Italy
Istituto di Biostrutture e Bioimmagini-Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, Napoli 80134, Italy
Department of Environmental Sciences, II University of Naples, via Vivaldi 43, Caserta 81100, Italy
References:
Not available.
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
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.
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.
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
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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
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11 Records (11 excluding Abstracts).
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Total impact factor: 45.262 (45.262 excluding Abstracts).
Total 5 year impact factor: 45.593 (45.593 excluding Abstracts).
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