Microscopic observations reveal that fusogenic peptides induce liposome shrinkage prior to membrane fusion

DOI Web Site 被引用文献12件
  • Fumimasa Nomura
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Takehiko Inaba
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Satoshi Ishikawa
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Miki Nagata
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Sho Takahashi
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Hirokazu Hotani
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan
  • Kingo Takiguchi
    Department of Molecular Biology, School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan; and Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan

説明

<jats:p>To study the mechanisms involved in membrane fusion, we visualized the fusion process of giant liposomes in real time by optical dark-field microscopy. To induce membrane fusion, we used (<jats:italic>i</jats:italic>) influenza hemagglutinin peptide (HA), a 20-aa peptide derived from the N-terminal fusion peptide region of the HA2 subunit, and (<jats:italic>ii</jats:italic>) two synthetic analogue peptides of HA, a negatively (E5) and positively (K5) charged analogue. We were able to visualize membrane fusion caused by E5 or by K5 alone, as well as by the mixture of these two peptides. The HA peptide however, did not induce membrane fusion, even at an acidic pH, which has been described as the optimal condition for the fusion of large unilamellar vesicles. Surprisingly, before membrane fusion, the shrinkage of liposomes was always observed. Our results suggest that a perturbation of lipid bilayers, which probably resulted from alterations in the bending folds of membranes, is a critical factor in fusion efficiency.</jats:p>

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