ArticleEuropean biophysics journal : EBJ2005
Viral membrane penetration: lytic activity of a nodaviral fusion peptide.
Article in European biophysics journal : EBJ, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Meet the IUPAB Councilor-Hans-Joachim Galla.Biophysical reviews · 2021Article
- Influence of membrane composition on the binding and folding of a membrane lytic peptide from the non-enveloped flock house virus.Biochimica et biophysica acta. Biomembranes · 2017Article
- Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.Advances in colloid and interface science · 2014Review
- Learning from the viral journey: how to enter cells and how to overcome intracellular barriers to reach the nucleus.The AAPS journal · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The auto-cleavage product from the C-terminal part of the capsid protein of the flock house virus, namely the gamma(1) peptide, was used as a model peptide to characterize the initial steps of viral membrane penetration. Monolayers at the air-water interface were used to investigate the phase behaviour of ternary lipid-peptide mixtures, whereas solid-supported membranes were used to visualize the lytic activity of the gamma(1) peptide. 1,2-Dipalmitoyl-sn-glycero-phospatidylcholine/1,2-dipalmitoyl-sn-glycero-phospatidylserine (4:1) membranes were used as negatively charged model membranes. By means of film balance techniques lipid/peptide discrimination was found resulting in a lipid-rich and a peptide-rich phase. Quartz crystal microbalance and scanning force microscopy experiments led to the conclusion of a detergent-like mechanism of the gamma(1) peptide resulting in mixed lipid-peptide micelles with a molar ratio of 2.8:1. A monolayer adsorption with an ongoing lysis of membranes was found with gamma(1) peptide molecules interacting at membrane defects.
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Registered trials
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