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Interaction of Influenza Virus Fusion Peptide with Lipid Membranes: Effect of Lysolipid

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Abstract

The effect of lysophosphatidylcholine (LPC) on lipid vesicle fusion and leakage induced by influenza virus fusion peptides and the peptide interaction with lipid membranes were studied by using fluorescence spectroscopy and monolayer surface tension measurements. It was confirmed that the wild-type fusion peptide-induced vesicle fusion rate increased several-fold between pH 7 and 5, unlike a mutated peptide, in which valine residues were substituted for glutamic acid residues at positions 11 and 15. This mutated peptide exhibited a much greater ability to induce lipid vesicle fusion and leakage but in a less pH-dependent manner compared to the wild-type fusion peptide. The peptide-induced vesicle fusion and leakage were well correlated with the degree of interaction of these peptides with lipid membranes, as deduced from the rotational correlation time obtained for the peptide tryptophan fluorescence. Both vesicle fusion and leakage induced by the peptides were suppressed by LPC incorporated into lipid vesicle membranes in a concentration-dependent manner. The rotational correlation time associated with the peptide’s tryptophan residue, which interacts with lipid membranes containing up to 25 mole % LPC, was virtually the same compared to lipid membranes without LPC, indicating that LPC-incorporated membrane did not affect the peptide interaction with the membrane. The adsorption of peptide onto a lipid monolayer also showed that the presence of LPC did not affect peptide adsorption.

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Abbreviations

ANTS:

1-aminonaphthalene–1,3,6-trisulfonic acid, sodium salt

DOPC:

dioleolyphosphatidylcholine

DOPE:

dioleoylphosphatidylethanolamine DPX, N,N′-p-xylene-bis-pyridinium bromide

E11V/E15V fusion peptide:

GLFGAIAGFIVNGWVGMIDG-amide

LPC:

1-stearoyl-2-hydroxy-phosphatidylcholine

LUV:

large unilamellar vesicles

NBD-PE:

N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-phosphatidylethanolamine

NCB:

0.15 M NaCl/10 mM Na citrate, pH 4.7 or 5.0

NHB:

150 mM NaCl/10 mM HEPES, pH 7.3 or 7.4

Rh-PE:

N-(lissamine rhodamine B sulphonyl)- phosphatidylethanolamine

SUV:

small unilamellar vesicles

NTB:

0.15 M NaCl/10 mM Tris, pH 7.4

WT-fusion peptide:

GLFGAIAGFIENGWEGMIDG-amide

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Acknowledgment

This work was funded in part by the Canadian Institutes for Health Research (grant MA-7654) to RME. FVB also acknowledges support from the National Science Foundation. GAB gratefully acknowledges ORNL for providing generous support of this work in the form of a Eugene P. Wigner Fellowship.

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Authors and Affiliations

  1. Department of Physiology & Biophysics, School of Medicine & Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY, 14214, USA

    S. Ohki

  2. Chemical Sciences Division, Oak Ridge National Laboratory, P.O. Box 2008, Oak Ridge, TN, 37831, USA

    G.A. Baker

  3. Department of Chemistry, College of Arts and Natural Sciences, University at Buffalo, The State University of New York, Buffalo, NY, 14260-3000, USA

    P.M. Page, T.A. McCarty & F.V. Bright

  4. Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, L8N 3Z5, Canada

    R.M. Epand

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  1. S. Ohki
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  2. G.A. Baker
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Correspondence to S. Ohki.

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Ohki, S., Baker, G., Page, P. et al. Interaction of Influenza Virus Fusion Peptide with Lipid Membranes: Effect of Lysolipid. J Membrane Biol 211, 191–200 (2006). https://doi.org/10.1007/s00232-006-0862-z

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  • DOI: https://doi.org/10.1007/s00232-006-0862-z

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