Inactivation of γ-Hemolysin Hyll Component by Addition of Monosialoganglioside GM1 to Human Erythrocyte1

Toshiko Ozawa, Jun Kaneko, Hirofumi Nariya, Kazuo Izaki, Yoshiyuki Kamio

    Research output: Contribution to journalArticlepeer-review

    14 Citations (Scopus)

    Abstract

    The Staphylococcal toxins leukocidin and γ-hemolysin consist of two protein components: F and S in leukocidin and Hγl and Hγll in γ-hemolysin. The two toxins share one component (F = Hγl). We found that the Hγll component was completely inactivated by the addition of monosialoganglioside GM1 at the molar ratio of 1:1. Disialogangliosides GD1a and GD1b had little effect on the inactivation of Hγll. The molar ratios of GD1a and GD1b to Hγll needed for maximum inactivation were 30:1 and 100:1, respectively. Related glycolipids caused little if any inactivation. Hγll bound to GM1 to form HγII-GM1 complexes.Analysis of the intrinsic aromatic amino acid fluorescence in Hγll and HγII-GM1 with 280 nm as the excitation wavelength showed that GM1 in the complex reduced the fluorescence intensity of Hγll by 12% without changing the wavelength of maximum emission (325 nm). We concluded that GM1 is a receptor of the Hγll component on human erythrocytes and that Hγll takes on a different conformation when it binds to GM1.

    Original languageEnglish
    Pages (from-to)602-605
    Number of pages4
    JournalBioscience, Biotechnology, and Biochemistry
    Volume58
    Issue number3
    DOIs
    Publication statusPublished - 1994

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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