ArticleJournal of virology2002
Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 104 citations in OpenAlex.
- Probing living cell dynamics and molecular interactions using atomic force microscopy.Biophysical reviews · 2024Review
- Interferon-stimulated gene PVRL4 broadly suppresses viral entry by inhibiting viral-cellular membrane fusion.Cell & bioscience · 2024Article
- Insights into Polyphenol-Lipid Interactions: Chemical Methods, Molecular Aspects and Their Effects on Membrane Structures.Plants (Basel, Switzerland) · 2022Review
- Interactions between Hydrolysable Tannins and Lipid Vesicles fromMolecules (Basel, Switzerland) · 2022Article
- Evaluation of Host Cell Impurity Effects on the Performance of Sterile Filtration Processes for Therapeutic Viruses.Membranes · 2022Article
- Scramblases as Regulators of ProteolyticMembranes · 2022Review
- Untargeted Lipidomics of Vesicular Stomatitis Virus-Infected Cells and Viral Particles.Viruses · 2021Article
- Physicochemical tools for studying virus interactions with targeted cell membranes in a molecular and spatiotemporally resolved context.Analytical and bioanalytical chemistry · 2021Review
- How virus size and attachment parameters affect the temperature sensitivity of virus binding to host cells: Predictions of a thermodynamic model for arboviruses and HIV.Microbial risk analysis · 2020Article
- Towards a thermodynamic mechanistic model for the effect of temperature on arthropod vector competence for transmission of arboviruses.Microbial risk analysis · 2019Article
- Using thermodynamic parameters to calibrate a mechanistic dose-response for infection of a host by a virus.Microbial risk analysis · 2018Article
- Virus stamping for targeted single-cell infection in vitro and in vivo.Nature biotechnology · 2018Article
- Fusion Stage of HIV-1 Entry Depends on Virus-Induced Cell Surface Exposure of Phosphatidylserine.Cell host & microbe · 2017Article
- Immobilized lentivirus vector on chondroitin sulfate-hyaluronate acid-silk fibroin hybrid scaffold for tissue-engineered ligament-bone junction.BioMed research international · 2014Article
- Understanding and altering cell tropism of vesicular stomatitis virus.Virus research · 2013Review
- Anionic lipids are required for vesicular stomatitis virus G protein-mediated single particle fusion with supported lipid bilayers.The Journal of biological chemistry · 2013Article
- Article
- Entry of rhabdoviruses into animal cells.Advances in experimental medicine and biology · 2013Review
- Oncolytic virotherapy for ovarian cancer.Oncolytic virotherapy · 2012Article
- Genetic inactivation of COPI coatomer separately inhibits vesicular stomatitis virus entry and gene expression.Journal of virology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vesicular stomatitis virus (VSV) infection depends on the fusion of viral and cellular membranes, which is mediated by virus spike glycoprotein G at the acidic environment of the endosomal compartment. VSV G protein does not contain a hydrophobic amino acid sequence similar to the fusion peptides found among other viral glycoproteins, suggesting that membrane recognition occurs through an alternative mechanism. Here we studied the interaction between VSV G protein and liposomes of different phospholipid composition by force spectroscopy, isothermal titration calorimetry (ITC), and fluorescence spectroscopy. Force spectroscopy experiments revealed the requirement for negatively charged phospholipids for VSV binding to membranes, suggesting that this interaction is electrostatic in nature. In addition, ITC experiments showed that VSV binding to liposomes is an enthalpically driven process. Fluorescence data also showed the lack of VSV interaction with the vesicles as well as inhibition of VSV-induced membrane fusion at high ionic strength. Intrinsic fluorescence measurements showed that the extent of G protein conformational changes depends on the presence of phosphatidylserine (PS) on the target membrane. Although the increase in PS content did not change the binding profile, the rate of the fusion reaction was remarkably increased when the PS content was increased from 25 to 75%. On the basis of these data, we suggest that G protein binding to the target membrane essentially depends on electrostatic interactions, probably between positive charges on the protein surface and negatively charged phospholipids in the cellular membrane. In addition, the fusion is exothermic, indicating no entropic constraints to this process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.