Probing the interaction between vesicular stomatitis virus and phosphatidylserine
The entry of enveloped animal viruses into their host cells always depends on membrane fusion triggered by conformational changes in viral envelope glycoproteins. Vesicular stomatitis virus (VSV) infection is mediated by virus spike glycoprotein G, which induces membrane fusion between the viral env...
Guardado en:
| Publicado: |
2006
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757571_v35_n2_p145_Carneiro http://hdl.handle.net/20.500.12110/paper_01757571_v35_n2_p145_Carneiro |
| Aporte de: |
| id |
paper:paper_01757571_v35_n2_p145_Carneiro |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_01757571_v35_n2_p145_Carneiro2023-06-08T15:18:55Z Probing the interaction between vesicular stomatitis virus and phosphatidylserine phosphatidylserine acidity article atomic force microscopy chemical interaction controlled study membrane fusion membrane transport molecular dynamics molecular probe nonhuman peptide synthesis pH measurement prediction spectrometry theoretical study Vesicular stomatitis virus Amino Acids Animals Calorimetry Cell Line Cell Membrane Computer Simulation Electrostatics Histidine Hydrogen-Ion Concentration Liposomes Membrane Glycoproteins Microscopy, Atomic Force Phosphatidylserines Protein Binding Thermodynamics Valine Vesicular stomatitis-Indiana virus Viral Envelope Proteins Viral Fusion Proteins Animalia Vesicular stomatitis virus The entry of enveloped animal viruses into their host cells always depends on membrane fusion triggered by conformational changes in viral envelope glycoproteins. Vesicular stomatitis virus (VSV) infection is mediated by virus spike glycoprotein G, which induces membrane fusion between the viral envelope and the endosomal membrane at the acidic environment of this compartment. In this work, we evaluated VSV interactions with membranes of different phospholipid compositions, at neutral and acidic pH, using atomic force microscopy (AFM) operating in the force spectroscopy mode, isothermal calorimetry (ITC) and molecular dynamics simulation. We found that the binding forces differed dramatically depending on the membrane phospholipid composition, revealing a high specificity of G protein binding to membranes containing phosphatidylserine (PS). In a previous work, we showed that the sequence corresponding amino acid 145-164 of VSV G protein was as efficient as the virus in catalyzing membrane fusion at pH 6.0. Here, we used this sequence to explore VSV-PS interaction using ITC. We found that peptide binding to membranes was exothermic, suggesting the participation of electrostatic interactions. Peptide-membrane interaction at pH 7.5 was shown to be specific to PS and dependent on the presence of His residues in the fusion peptide. The application of the simplified continuum Gouy-Chapman theory to our system predicted a pH of 5.0 at membrane surface, suggesting that the His residues should be protonated when located close to the membrane. Molecular dynamics simulations suggested that the peptide interacts with the lipid bilayer through its N-terminal residues, especially Val145 and His148. © EBSA 2005. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757571_v35_n2_p145_Carneiro http://hdl.handle.net/20.500.12110/paper_01757571_v35_n2_p145_Carneiro |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
phosphatidylserine acidity article atomic force microscopy chemical interaction controlled study membrane fusion membrane transport molecular dynamics molecular probe nonhuman peptide synthesis pH measurement prediction spectrometry theoretical study Vesicular stomatitis virus Amino Acids Animals Calorimetry Cell Line Cell Membrane Computer Simulation Electrostatics Histidine Hydrogen-Ion Concentration Liposomes Membrane Glycoproteins Microscopy, Atomic Force Phosphatidylserines Protein Binding Thermodynamics Valine Vesicular stomatitis-Indiana virus Viral Envelope Proteins Viral Fusion Proteins Animalia Vesicular stomatitis virus |
| spellingShingle |
phosphatidylserine acidity article atomic force microscopy chemical interaction controlled study membrane fusion membrane transport molecular dynamics molecular probe nonhuman peptide synthesis pH measurement prediction spectrometry theoretical study Vesicular stomatitis virus Amino Acids Animals Calorimetry Cell Line Cell Membrane Computer Simulation Electrostatics Histidine Hydrogen-Ion Concentration Liposomes Membrane Glycoproteins Microscopy, Atomic Force Phosphatidylserines Protein Binding Thermodynamics Valine Vesicular stomatitis-Indiana virus Viral Envelope Proteins Viral Fusion Proteins Animalia Vesicular stomatitis virus Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| topic_facet |
phosphatidylserine acidity article atomic force microscopy chemical interaction controlled study membrane fusion membrane transport molecular dynamics molecular probe nonhuman peptide synthesis pH measurement prediction spectrometry theoretical study Vesicular stomatitis virus Amino Acids Animals Calorimetry Cell Line Cell Membrane Computer Simulation Electrostatics Histidine Hydrogen-Ion Concentration Liposomes Membrane Glycoproteins Microscopy, Atomic Force Phosphatidylserines Protein Binding Thermodynamics Valine Vesicular stomatitis-Indiana virus Viral Envelope Proteins Viral Fusion Proteins Animalia Vesicular stomatitis virus |
| description |
The entry of enveloped animal viruses into their host cells always depends on membrane fusion triggered by conformational changes in viral envelope glycoproteins. Vesicular stomatitis virus (VSV) infection is mediated by virus spike glycoprotein G, which induces membrane fusion between the viral envelope and the endosomal membrane at the acidic environment of this compartment. In this work, we evaluated VSV interactions with membranes of different phospholipid compositions, at neutral and acidic pH, using atomic force microscopy (AFM) operating in the force spectroscopy mode, isothermal calorimetry (ITC) and molecular dynamics simulation. We found that the binding forces differed dramatically depending on the membrane phospholipid composition, revealing a high specificity of G protein binding to membranes containing phosphatidylserine (PS). In a previous work, we showed that the sequence corresponding amino acid 145-164 of VSV G protein was as efficient as the virus in catalyzing membrane fusion at pH 6.0. Here, we used this sequence to explore VSV-PS interaction using ITC. We found that peptide binding to membranes was exothermic, suggesting the participation of electrostatic interactions. Peptide-membrane interaction at pH 7.5 was shown to be specific to PS and dependent on the presence of His residues in the fusion peptide. The application of the simplified continuum Gouy-Chapman theory to our system predicted a pH of 5.0 at membrane surface, suggesting that the His residues should be protonated when located close to the membrane. Molecular dynamics simulations suggested that the peptide interacts with the lipid bilayer through its N-terminal residues, especially Val145 and His148. © EBSA 2005. |
| title |
Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| title_short |
Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| title_full |
Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| title_fullStr |
Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| title_full_unstemmed |
Probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| title_sort |
probing the interaction between vesicular stomatitis virus and phosphatidylserine |
| publishDate |
2006 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01757571_v35_n2_p145_Carneiro http://hdl.handle.net/20.500.12110/paper_01757571_v35_n2_p145_Carneiro |
| _version_ |
1768545046720675840 |