ArticleThe Journal of biological chemistry2010
NMR structure of a viral peptide inserted in artificial membranes: a view on the early steps of the birnavirus entry process.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Plasmon Waveguide Resonance: Principles, Applications and Historical Perspectives on Instrument Development.Molecules (Basel, Switzerland) · 2021Review
- Phosphatidylinositol 3-Phosphate Mediates the Establishment of Infectious Bursal Disease Virus Replication Complexes in Association with Early Endosomes.Journal of virology · 2021Article
- The RNA-Binding Protein of a Double-Stranded RNA Virus Acts like a Scaffold Protein.Journal of virology · 2018Article
- Membranotropic peptides mediating viral entry.Peptide science (Hoboken, N.J.) · 2018Review
- The bacteriophage ϕ29 tail possesses a pore-forming loop for cell membrane penetration.Nature · 2016Article
- Three-dimensional structure of a protozoal double-stranded RNA virus that infects the enteric pathogen Giardia lamblia.Journal of virology · 2015Article
- Exploitation of viral properties for intracellular delivery.Journal of peptide science : an official publication of the European Peptide Society · 2014Review
- Peptide-lipid interactions: experiments and applications.International journal of molecular sciences · 2013Article
- Modeling the interaction of dodecylphosphocholine micelles with the anticoccidial peptide PW2 guided by NMR data.Molecules (Basel, Switzerland) · 2013Article
- Dissecting quasi-equivalence in nonenveloped viruses: membrane disruption is promoted by lytic peptides released from subunit pentamers, not hexamers.Journal of virology · 2012Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonenveloped virus must penetrate the cellular membrane to access the cytoplasm without the benefit of membrane fusion. For birnavirus, one of the peptides present in the virus capsid, pep46 for infectious bursal disease virus, is able to induce pores into membranes as an intermediate step of the birnavirus-penetration pathway. Using osmotic protection experiments, we demonstrate here that pep46 and its pore-forming N-terminal moiety (pep22) form pores of different diameters, 5-8 and 2-4 nm, respectively, showing that both pep46 moieties participate to pore formation. The solution structures of pep46, pep22, and pep24 (the pep46 C-terminal moiety) in different hydrophobic environments and micelles determined by (1)H NMR studies provide structural insights of the pep46 domain interaction. In CDCl(3)/CD(3)OH mixture and in dodecylphosphocholine micelles, the N-terminal domain of pep46 is structured in a long kinked helix, although the C terminus is structured in one or two helices depending upon the solvents used. We also show that the folding and the proline isomerization status of pep46 depend on the type of hydrophobic environment. NMR spectroscopy with labeled phospholipid micelles, differential scanning calorimetry, and plasmon waveguide resonance studies show the peptides lie parallel to the lipid-water interface, perturbing the fatty acid chain packing. All these data lead to a model in which the two domains of pep46 interact with the membrane to form pores.
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