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
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Publicado: Public Library of Science (PLoS) 2012
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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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