Sequential Binding of Staphylococcal y-Hemolysin to Human Erythrocytes and Complex Formation of the Hemolysin on the Cell Surface

Jun Kaneko, Toshiko Ozawa, Toshio Tomita, Yoshiyuki Kamio

研究成果: Article査読

32 被引用数 (Scopus)

抄録

Staphylococcal γ-hemolysin consists of two protein components, F (or HγI) and HγII. To elucidate the mode of action of γ-hemolysin, we studied the binding order of F and HγII to human erythrocytes and the cell-bound state of the two components. The binding of F to human erythrocytes preceded the binding of HγII to the cells, and thereafter hemolysis occurred. Western immunoblot analysis of the cell-bound γ-hemolysin indicated that F and HγII components form high-molecular-mass (150–250 kDa) complexes on the erythrocytes. The toxin complexes were recovered in a Triton X-100-insoluble fraction of the erythrocytes, which contains cytoskeleton proteins. Neither the formation of the toxin complex(es) nor hemolysis occurred when the erythrocytes were treated with proteinase K. Abortion of the complex formation on the proteinase K-treated erythrocytes may be due to the failure of the binding of HγII to the cells, because F bound to the proteinase K-treated erythrocytes to the same extent as to the non-treated erythrocytes.

本文言語English
ページ(範囲)846-851
ページ数6
ジャーナルBioscience, Biotechnology and Biochemistry
61
5
DOI
出版ステータスPublished - 1997 1

ASJC Scopus subject areas

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

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