Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process(747 views) Galdiero S, Falanga A, Vitiello G, Vitiello M, Pedone C, D'Errico G, Galdiero M
Department of Biological Sciences, Division of Biostructures - University of Naples Federico II, Via Mezzocannone 16, 80134, Napoli, Italy.
Centro Interuniversitario, Ricerca sui Peptidi Bioattivi - University of Naples Federico II, Via Mezzocannone 16, 80134 Napoli, Italy
Istituto di Biostrutture, Bioimmagini - CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Department of Chemistry, University of Naples Federico II, CSGI - Monte Sant'Angelo, 80126 Napoli, Italy
Consorzio per lo Studio dei Sistemi a Grande Interfase, CSGI - Monte Sant'Angelo, 80126 Napoli, Italy
Department of Experimental Medicine - II University of Naples, Via De Crecchio 7, 80138 Napoli, Italy
References: Not available.
Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process
The entry of enveloped viruses involves attachment followed by close apposition of the viral and plasma membranes. Then, either on the cell surface or in an endocytotic vesicle, the two membranes fuse by an energetically unfavourable process requiring the destabilisation of membrane microenvironment in order to release the viral nucleocapsid into the cytoplasm. The core fusion machinery, conserved throughout the herpesvirus family, involves glycoprotein B (gB) and the non-covalently associated complex of glycoproteins H and L (gH/gL). Both gB and gH possess several hydrophobic domains necessary for efficient induction of fusion, and synthetic peptides corresponding to these regions are able to associate to membranes and induce fusion of artificial liposomes. Here, we describe the first application of surface plasmon resonance (SPR) to the study of the interaction of viral membranotropic peptides with model membranes in order to enhance our molecular understanding of the mechanism of membrane fusion. SPR spectroscopy data are supported by tryptophan fluorescence, circular dichroism and electron spin resonance spectroscopy (ESR). We selected peptides from gB and gH and also analysed the behaviour of HIV gp41 fusion peptide and the cationic antimicrobial peptide melittin. The combined results of SPR and ESR showed a marked difference between the mode of action of the HSV peptides and the HIV fusion peptide compared to melittin, suggesting that viral-derived membrane interacting peptides all act via a similar mechanism, which is substantially different from that of the non-cell selective lytic peptide melittin. Copyright 2010 Elsevier B.V. All rights reserved.
Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process
Petraglia F, Singh AA, Carafa V, Nebbioso A, Conte M, Scisciola L, Valente S, Baldi A, Mandoli A, Petrizzi VB, Ingenito C, De Falco S, Cicatiello V, Apicella I, Janssen-megens EM, Kim B, Yi G, Logie C, Heath S, Ruvo M, Wierenga ATJ, Flicek P, Yaspo ML, Della Valle V, Bernard O, Tomassi S, Novellino E, Feoli A, Sbardella G, Gut I, Vellenga E, Stunnenberg HG, Mai A, Martens JHA, Altucci L * Combined HAT/EZH2 modulation leads to cancer-selective cell death(451 views) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 ViewExport to BibTeXExport to EndNote