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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