Probing the interaction between vesicular stomatitis virus and phosphatidylserine

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dc.contributor.author Carneiro, F. A.
dc.contributor.author Lapido-Loureiro, P. A.
dc.contributor.author Cordo, S. M.
dc.contributor.author Stauffer, F.
dc.contributor.author Weissmuller, G.
dc.contributor.author Bianconi, M. L.
dc.contributor.author Juliano, M. A.
dc.contributor.author Juliano, L.
dc.contributor.author Bisch, P. M.
dc.contributor.author Poian, ATD
dc.date.accessioned 2016-01-24T12:38:15Z
dc.date.available 2016-01-24T12:38:15Z
dc.date.issued 2006-01-01
dc.identifier http://dx.doi.org/10.1007/s00249-005-0012-z
dc.identifier.citation European Biophysics Journal With Biophysics Letters. New York: Springer, v. 35, n. 2, p. 145-154, 2006.
dc.identifier.issn 0175-7571
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/28631
dc.description.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). en
dc.format.extent 145-154
dc.language.iso eng
dc.publisher Springer
dc.relation.ispartof European Biophysics Journal With Biophysics Letters
dc.rights Acesso restrito
dc.subject membrane fusion en
dc.subject visicular stomatitis virus en
dc.subject phosphatidylserine en
dc.subject histidine en
dc.title Probing the interaction between vesicular stomatitis virus and phosphatidylserine en
dc.type Artigo
dc.rights.license http://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.contributor.institution Universidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institution Univ Buenos Aires
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Univ Fed Rio de Janeiro, Inst Bioquim Med, BR-21941590 Rio de Janeiro, Brazil
dc.description.affiliation Univ Fed Rio de Janeiro, Lab Fis Biol, Inst Biofis Carlos Chagas Filho, BR-21949900 Rio de Janeiro, Brazil
dc.description.affiliation Univ Buenos Aires, Fac Ciencias Exactas & Nat, Virol Lab, Dept Quim Biol, Buenos Aires, DF, Argentina
dc.description.affiliation UNIFESP, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp UNIFESP, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.identifier.doi 10.1007/s00249-005-0012-z
dc.description.source Web of Science
dc.identifier.wos WOS:000234409800006



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