tetano
Editor, Senior Moderator
Biochim Biophys Acta. 2016 Nov 4. pii: S0304-4165(16)30407-X. doi: 10.1016/j.bbagen.2016.11.004. [Epub ahead of print]
[h=1]Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface.[/h] Worch R[SUP]1[/SUP], Krupa J[SUP]2[/SUP], Filipek A[SUP]2[/SUP], Szymaniec A[SUP]2[/SUP], Setny P[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The N-terminal fragment of the viral hemagglutinin HA2 subunit is termed a fusion peptide (HAfp). The 23-amino acid peptide (HAfp1-23) contains three C-terminal W21-Y22-G23 residues which are highly conserved among serotypes of influenza A and has been shown to form a tight helical hairpin very distinct from the boomerang structure of HAfp1-20. We studied the effect of peptide length on fusion properties, structural dynamics, and binding to the membrane interface. We developed a novel fusion visualization assay based on FLIM microscopy on giant unilamellar vesicles (GUV). By means of molecular dynamics simulations and spectroscopic measurements, we show that the presence of the three C-terminal W21-Y22-G23 residues promotes the hairpin formation, which orients perpendicularly to the membrane plane and induces more disorder in the surrounding lipids than the less structured HAfp1-20. Moreover, we report cholesterol-enriched domain formation induced exclusively by the longer fusion peptide.
Copyright ? 2016. Published by Elsevier B.V.
[h=4]KEYWORDS:[/h] confocal microscopy; fluorescence; giant unilamellar vesicles; influenza virus; lifetime imaging microscopy; molecular simulations; peptide-lipid interactions
PMID: 27825831 DOI: 10.1016/j.bbagen.2016.11.004
[PubMed - as supplied by publisher]
[h=1]Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface.[/h] Worch R[SUP]1[/SUP], Krupa J[SUP]2[/SUP], Filipek A[SUP]2[/SUP], Szymaniec A[SUP]2[/SUP], Setny P[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The N-terminal fragment of the viral hemagglutinin HA2 subunit is termed a fusion peptide (HAfp). The 23-amino acid peptide (HAfp1-23) contains three C-terminal W21-Y22-G23 residues which are highly conserved among serotypes of influenza A and has been shown to form a tight helical hairpin very distinct from the boomerang structure of HAfp1-20. We studied the effect of peptide length on fusion properties, structural dynamics, and binding to the membrane interface. We developed a novel fusion visualization assay based on FLIM microscopy on giant unilamellar vesicles (GUV). By means of molecular dynamics simulations and spectroscopic measurements, we show that the presence of the three C-terminal W21-Y22-G23 residues promotes the hairpin formation, which orients perpendicularly to the membrane plane and induces more disorder in the surrounding lipids than the less structured HAfp1-20. Moreover, we report cholesterol-enriched domain formation induced exclusively by the longer fusion peptide.
Copyright ? 2016. Published by Elsevier B.V.
[h=4]KEYWORDS:[/h] confocal microscopy; fluorescence; giant unilamellar vesicles; influenza virus; lifetime imaging microscopy; molecular simulations; peptide-lipid interactions
PMID: 27825831 DOI: 10.1016/j.bbagen.2016.11.004
[PubMed - as supplied by publisher]