Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.

The molecular mechanism of entry of herpesviruses requires a multicomponent fusion system. Cell invasion by Herpes simplex virus (HSV) requires four virally encoded glycoproteins: namely gD, gB and gH/gL. The role of gB has remained elusive until recently when the crystal structure of HSV-1 gB becam...

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Autores principales:	Annarita Falanga, Rossella Tarallo, Giuseppe Vitiello, Mariateresa Vitiello, Emiliana Perillo, Marco Cantisani, Gerardino D'Errico, Massimiliano Galdiero, Stefania Galdiero
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/415c9aee102c4bedb37923a9df19e764
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spelling	oai:doaj.org-article:415c9aee102c4bedb37923a9df19e7642021-11-18T07:26:53ZBiophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.1932-620310.1371/journal.pone.0032186https://doaj.org/article/415c9aee102c4bedb37923a9df19e7642012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22384173/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The molecular mechanism of entry of herpesviruses requires a multicomponent fusion system. Cell invasion by Herpes simplex virus (HSV) requires four virally encoded glycoproteins: namely gD, gB and gH/gL. The role of gB has remained elusive until recently when the crystal structure of HSV-1 gB became available and the fusion potential of gB was clearly demonstrated. Although much information on gB structure/function relationship has been gathered in recent years, the elucidation of the nature of the fine interactions between gB fusion loops and the membrane bilayer may help to understand the precise molecular mechanism behind herpesvirus-host cell membrane fusion. Here, we report the first biophysical study on the two fusion peptides of gB, with a particular focus on the effects determined by both peptides on lipid bilayers of various compositions. The two fusion loops constitute a structural subdomain wherein key hydrophobic amino acids form a ridge that is supported on both sides by charged residues. When used together the two fusion loops have the ability to significantly destabilize the target membrane bilayer, notwithstanding their low bilayer penetration when used separately. These data support the model of gB fusion loops insertion into cholesterol enriched membranes.Annarita FalangaRossella TaralloGiuseppe VitielloMariateresa VitielloEmiliana PerilloMarco CantisaniGerardino D'ErricoMassimiliano GaldieroStefania GaldieroPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e32186 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Annarita Falanga Rossella Tarallo Giuseppe Vitiello Mariateresa Vitiello Emiliana Perillo Marco Cantisani Gerardino D'Errico Massimiliano Galdiero Stefania Galdiero Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
description	The molecular mechanism of entry of herpesviruses requires a multicomponent fusion system. Cell invasion by Herpes simplex virus (HSV) requires four virally encoded glycoproteins: namely gD, gB and gH/gL. The role of gB has remained elusive until recently when the crystal structure of HSV-1 gB became available and the fusion potential of gB was clearly demonstrated. Although much information on gB structure/function relationship has been gathered in recent years, the elucidation of the nature of the fine interactions between gB fusion loops and the membrane bilayer may help to understand the precise molecular mechanism behind herpesvirus-host cell membrane fusion. Here, we report the first biophysical study on the two fusion peptides of gB, with a particular focus on the effects determined by both peptides on lipid bilayers of various compositions. The two fusion loops constitute a structural subdomain wherein key hydrophobic amino acids form a ridge that is supported on both sides by charged residues. When used together the two fusion loops have the ability to significantly destabilize the target membrane bilayer, notwithstanding their low bilayer penetration when used separately. These data support the model of gB fusion loops insertion into cholesterol enriched membranes.
format	article
author	Annarita Falanga Rossella Tarallo Giuseppe Vitiello Mariateresa Vitiello Emiliana Perillo Marco Cantisani Gerardino D'Errico Massimiliano Galdiero Stefania Galdiero
author_facet	Annarita Falanga Rossella Tarallo Giuseppe Vitiello Mariateresa Vitiello Emiliana Perillo Marco Cantisani Gerardino D'Errico Massimiliano Galdiero Stefania Galdiero
author_sort	Annarita Falanga
title	Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
title_short	Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
title_full	Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
title_fullStr	Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
title_full_unstemmed	Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.
title_sort	biophysical characterization and membrane interaction of the two fusion loops of glycoprotein b from herpes simplex type i virus.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/415c9aee102c4bedb37923a9df19e764
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Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.

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