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Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
Published on: January 2, 2014
Probing the interaction between vesicular stomatitis virus and phosphatidylserine
Fabiana A Carneiro1, Pedro A Lapido-Loureiro, Sandra M Cordo
1Instituto de Bioquìmica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-590, Brazil.
European Biophysics Journal : EBJ
|September 27, 2005
Summary
Vesicular stomatitis virus (VSV) glycoprotein G specifically binds to phosphatidylserine (PS) on host cell membranes. This interaction, crucial for viral entry, is mediated by electrostatic forces and specific amino acids within the G protein.
Area of Science:
- Virology
- Biophysics
- Structural Biology
Background:
- Enveloped viruses enter cells via membrane fusion, a process driven by viral glycoproteins.
- Vesicular stomatitis virus (VSV) uses its glycoprotein G to fuse with endosomal membranes in an acidic environment.
Purpose of the Study:
- To investigate the interaction between VSV glycoprotein G and host cell membranes with varying phospholipid compositions.
- To elucidate the role of pH and specific amino acids in VSV-G protein-membrane interactions and fusion.
Main Methods:
- Atomic force microscopy (AFM) in force spectroscopy mode.
- Isothermal titration calorimetry (ITC).
- Molecular dynamics (MD) simulations.
- Application of Gouy-Chapman theory.
Main Results:
- VSV G protein exhibits high binding specificity for membranes containing phosphatidylserine (PS).
- Peptide derived from VSV G protein shows exothermic binding to PS membranes, indicating electrostatic interactions.
- Interaction is pH-dependent and requires histidine residues; simulations pinpoint N-terminal residues Val(145) and His(148) as key interaction points.
Conclusions:
- Phosphatidylserine is a critical determinant for VSV G protein binding to membranes.
- Electrostatic interactions and histidine protonation are vital for VSV-G protein-membrane recognition and fusion.
- Specific amino acid residues in the VSV G protein mediate its interaction with the lipid bilayer.
