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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| Veröffentlicht in: | PloS one 2012-02, Vol.7 (2), p.e32186-e32186 |
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| creator | Falanga, Annarita Tarallo, Rossella Vitiello, Giuseppe Vitiello, Mariateresa Perillo, Emiliana Cantisani, Marco D'Errico, Gerardino Galdiero, Massimiliano Galdiero, Stefania |
| 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. |
| doi_str_mv | 10.1371/journal.pone.0032186 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0032186</identifier><identifier>PMID: 22384173</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acrylamide - chemistry ; Amino Acid Motifs ; Amino acids ; Biochemistry ; Biology ; Biophysics - methods ; Cell fusion ; Chemistry ; Cholesterol ; Coding ; Crystal structure ; Crystallography, X-Ray - methods ; Glycoprotein B ; Glycoproteins ; Herpes simplex ; Herpes viruses ; Herpesvirus 1, Human - chemistry ; Herpesvirus 1, Human - metabolism ; Hydrophobicity ; Insertion ; Lipid bilayers ; Lipids ; Lipids - chemistry ; Medicine ; Membrane fusion ; Membranes ; Peptides ; Peptides - chemistry ; Protein Structure, Secondary ; Proteins ; Quantum dots ; Sensors ; Spectrometry, Fluorescence - methods ; Structure-function relationships ; Tryptophan - chemistry ; Tyrosine - chemistry ; Viral Envelope Proteins - chemistry ; Viruses</subject><ispartof>PloS one, 2012-02, Vol.7 (2), p.e32186-e32186</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Falanga et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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. 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These data support the model of gB fusion loops insertion into cholesterol enriched membranes.</description><subject>Acrylamide - chemistry</subject><subject>Amino Acid Motifs</subject><subject>Amino acids</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Biophysics - methods</subject><subject>Cell fusion</subject><subject>Chemistry</subject><subject>Cholesterol</subject><subject>Coding</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray - methods</subject><subject>Glycoprotein B</subject><subject>Glycoproteins</subject><subject>Herpes simplex</subject><subject>Herpes viruses</subject><subject>Herpesvirus 1, Human - chemistry</subject><subject>Herpesvirus 1, Human - metabolism</subject><subject>Hydrophobicity</subject><subject>Insertion</subject><subject>Lipid bilayers</subject><subject>Lipids</subject><subject>Lipids - chemistry</subject><subject>Medicine</subject><subject>Membrane fusion</subject><subject>Membranes</subject><subject>Peptides</subject><subject>Peptides - 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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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22384173</pmid><doi>10.1371/journal.pone.0032186</doi><tpages>e32186</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acrylamide - chemistry Amino Acid Motifs Amino acids Biochemistry Biology Biophysics - methods Cell fusion Chemistry Cholesterol Coding Crystal structure Crystallography, X-Ray - methods Glycoprotein B Glycoproteins Herpes simplex Herpes viruses Herpesvirus 1, Human - chemistry Herpesvirus 1, Human - metabolism Hydrophobicity Insertion Lipid bilayers Lipids Lipids - chemistry Medicine Membrane fusion Membranes Peptides Peptides - chemistry Protein Structure, Secondary Proteins Quantum dots Sensors Spectrometry, Fluorescence - methods Structure-function relationships Tryptophan - chemistry Tyrosine - chemistry Viral Envelope Proteins - chemistry Viruses |
| title | Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus |
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