Herpes simplex virus type 1 (HSV-1) induced membrane fusion remain one of the most elusive mechanisms to be decifered 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 (gL), 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 represent 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 α-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 H / Galdiero, Stefania; Falanga, Annarita; Vitiello, M.; Raiola, L.; Russo, L.; Pedone, Carlo; Isernia, C.; Galdiero, M.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 285:22(2010), pp. 17123-17136. [10.1074/jbc.M110.114819]

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.

GALDIERO, STEFANIA
;
FALANGA, ANNARITA;M. Vitiello;PEDONE, CARLO;
2010

Abstract

Herpes simplex virus type 1 (HSV-1) induced membrane fusion remain one of the most elusive mechanisms to be decifered 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 (gL), 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 represent 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 α-helical domain with high fusion propensity.
2010
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 / Galdiero, Stefania; Falanga, Annarita; Vitiello, M.; Raiola, L.; Russo, L.; Pedone, Carlo; Isernia, C.; Galdiero, M.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 285:22(2010), pp. 17123-17136. [10.1074/jbc.M110.114819]
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 / Galdiero, Stefania; Falanga, Annarita; Vitiello, M.; Raiola, L.; Russo, L.; Pedone, Carlo; Isernia, C.; Galdiero, M.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 285:22(2010), pp. 17123-17136. [10.1074/jbc.M110.114819]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/382303
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