Probing the interaction between vesicular stomatitis virus and phosphatidylserine

Probing the interaction between vesicular stomatitis virus and phosphatidylserine

Author Carneiro, F. A. Google Scholar
Lapido-Loureiro, P. A. Google Scholar
Cordo, S. M. Google Scholar
Stauffer, F. Google Scholar
Weissmuller, G. Google Scholar
Bianconi, M. L. Google Scholar
Juliano, M. A. Google Scholar
Juliano, L. Google Scholar
Bisch, P. M. Google Scholar
Poian, ATD Google Scholar
Institution Universidade Federal do Rio de Janeiro (UFRJ)
Univ Buenos Aires
Universidade Federal de São Paulo (UNIFESP)
Abstract 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 Val(145) and His(148).
Keywords membrane fusion
visicular stomatitis virus
phosphatidylserine
histidine
Language English
Date 2006-01-01
Published in European Biophysics Journal With Biophysics Letters. New York: Springer, v. 35, n. 2, p. 145-154, 2006.
ISSN 0175-7571 (Sherpa/Romeo, impact factor)
Publisher Springer
Extent 145-154
Origin http://dx.doi.org/10.1007/s00249-005-0012-z
Access rights Closed access
Type Article
Web of Science ID WOS:000234409800006
URI http://repositorio.unifesp.br/handle/11600/28631

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