Substitution of Lysine for Arginine in the N-Terminal 217th Amino Acid Residue of the hγII of Staphylococcal γ-Hemolysin Lowers the Activity of the Toxin

Keiichi Sudo, Wanna Choorit, Ikuno Asami, Jun Kaneko, Koji Muramoto, Yoshiyuki Kamio

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The staphyloccocal toxin γ-hemolysin consists of two protein components, LukF and HγII. Staphylococcus aureus P83 was found to have five components, LukF, LukF-PV, LukM, LukS, and HγII for leukocidin orγ-hemolysin. HγII of S. aureus P83 was demonstrated to be a naturally-occurring analogous molecule of HγII [HγII(P83)], in which the 217th arginine residue was replaced by lysine. The HγII(P83) showed about 50% of the hemolytic activity of normal HγII in the presence of LukF.

Original languageEnglish
Pages (from-to)1786-1789
Number of pages4
JournalBioscience, Biotechnology, and Biochemistry
Volume59
Issue number9
DOIs
Publication statusPublished - 1995

ASJC Scopus subject areas

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

Fingerprint Dive into the research topics of 'Substitution of Lysine for Arginine in the N-Terminal 217th Amino Acid Residue of the hγII of Staphylococcal γ-Hemolysin Lowers the Activity of the Toxin'. Together they form a unique fingerprint.

Cite this