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...
Guardado en:
Autores principales: | , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/415c9aee102c4bedb37923a9df19e764 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:415c9aee102c4bedb37923a9df19e764 |
---|---|
record_format |
dspace |
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 |
work_keys_str_mv |
AT annaritafalanga biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT rossellatarallo biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT giuseppevitiello biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT mariateresavitiello biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT emilianaperillo biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT marcocantisani biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT gerardinoderrico biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT massimilianogaldiero biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus AT stefaniagaldiero biophysicalcharacterizationandmembraneinteractionofthetwofusionloopsofglycoproteinbfromherpessimplextypeivirus |
_version_ |
1718423404225232896 |