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Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface

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  • Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface

    Biochim Biophys Acta. 2016 Nov 4. pii: S0304-4165(16)30407-X. doi: 10.1016/j.bbagen.2016.11.004. [Epub ahead of print]
    Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface.

    Worch R1, Krupa J2, Filipek A2, Szymaniec A2, Setny P3.
    Author information

    Abstract

    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.


    KEYWORDS:

    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]
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