Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire
The implication of fusion peptides of class I viral fusion glycoproteins in the membrane fusion. Viral infection involves fusion between the viral envelope and the target cell plasmic membrane. The fusion is induced by a glycoprotein anchored in the viral envelope. After activation, the glycoprotein...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Presses Agronomiques de Gembloux
2007-01-01
|
| Series: | Biotechnologie, Agronomie, Société et Environnement |
| Subjects: | |
| Online Access: | http://www.pressesagro.be/base/text/v11n4/313.pdf |
| _version_ | 1818487707249147904 |
|---|---|
| author | Brasseur R. Charloteaux B. Lins L. Lorin A. |
| author_facet | Brasseur R. Charloteaux B. Lins L. Lorin A. |
| author_sort | Brasseur R. |
| collection | DOAJ |
| description | The implication of fusion peptides of class I viral fusion glycoproteins in the membrane fusion. Viral infection involves fusion between the viral envelope and the target cell plasmic membrane. The fusion is induced by a glycoprotein anchored in the viral envelope. After activation, the glycoprotein undergoes a conformational change inducing the exposure of a region named « fusion peptide » essential for the fusion process. Studies on glycoproteins and on isolated fusion peptides have allowed to better understand the mechanisms involved in membrane fusion. It was notably shown that fusion peptides induce fusion and leakage of membranes. These peptides are able to insert obliquely in a membrane when helical. This orientation induces lipid destabilisation, favouring membrane fusion. However, to date, none of these in vitro, in vivo or in silico studies has determined the minimal sequence required for membrane fusion. Using the obliquity-fusogenicity relationship, the latter was determined by molecular modelling for two viruses, the Human Immunodeficiency Virus and the Bovine Leukaemia Virus. These new results are of particular interest in the development of vaccines and antiviral drugs. |
| first_indexed | 2024-12-10T16:41:37Z |
| format | Article |
| id | doaj.art-e59cb2a25048421bb0e15bce4a86d30e |
| institution | Directory Open Access Journal |
| issn | 1370-6233 1780-4507 |
| language | English |
| last_indexed | 2024-12-10T16:41:37Z |
| publishDate | 2007-01-01 |
| publisher | Presses Agronomiques de Gembloux |
| record_format | Article |
| series | Biotechnologie, Agronomie, Société et Environnement |
| spelling | doaj.art-e59cb2a25048421bb0e15bce4a86d30e2022-12-22T01:41:12ZengPresses Agronomiques de GemblouxBiotechnologie, Agronomie, Société et Environnement1370-62331780-45072007-01-01114313335Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaireBrasseur R.Charloteaux B.Lins L.Lorin A.The implication of fusion peptides of class I viral fusion glycoproteins in the membrane fusion. Viral infection involves fusion between the viral envelope and the target cell plasmic membrane. The fusion is induced by a glycoprotein anchored in the viral envelope. After activation, the glycoprotein undergoes a conformational change inducing the exposure of a region named « fusion peptide » essential for the fusion process. Studies on glycoproteins and on isolated fusion peptides have allowed to better understand the mechanisms involved in membrane fusion. It was notably shown that fusion peptides induce fusion and leakage of membranes. These peptides are able to insert obliquely in a membrane when helical. This orientation induces lipid destabilisation, favouring membrane fusion. However, to date, none of these in vitro, in vivo or in silico studies has determined the minimal sequence required for membrane fusion. Using the obliquity-fusogenicity relationship, the latter was determined by molecular modelling for two viruses, the Human Immunodeficiency Virus and the Bovine Leukaemia Virus. These new results are of particular interest in the development of vaccines and antiviral drugs.http://www.pressesagro.be/base/text/v11n4/313.pdfHIVlipid bilayermolecular modellingsecondary structuretilted peptideviral infection |
| spellingShingle | Brasseur R. Charloteaux B. Lins L. Lorin A. Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire Biotechnologie, Agronomie, Société et Environnement HIV lipid bilayer molecular modelling secondary structure tilted peptide viral infection |
| title | Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire |
| title_full | Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire |
| title_fullStr | Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire |
| title_full_unstemmed | Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire |
| title_short | Implication des peptides de fusion des glycoprotéines de fusion virales de classe I dans la fusion membranaire |
| title_sort | implication des peptides de fusion des glycoproteines de fusion virales de classe i dans la fusion membranaire |
| topic | HIV lipid bilayer molecular modelling secondary structure tilted peptide viral infection |
| url | http://www.pressesagro.be/base/text/v11n4/313.pdf |
| work_keys_str_mv | AT brasseurr implicationdespeptidesdefusiondesglycoproteinesdefusionviralesdeclasseidanslafusionmembranaire AT charloteauxb implicationdespeptidesdefusiondesglycoproteinesdefusionviralesdeclasseidanslafusionmembranaire AT linsl implicationdespeptidesdefusiondesglycoproteinesdefusionviralesdeclasseidanslafusionmembranaire AT lorina implicationdespeptidesdefusiondesglycoproteinesdefusionviralesdeclasseidanslafusionmembranaire |