Substitution of lysine for arginine in the N-terminal 217th amino acid residue of the H gamma II of Staphylococcal gamma-hemolysin lowers the activity of the toxin

K Sudo; W Choorit; I Asami; J Kaneko; K Muramoto; Y Kamio

doi:10.1271/bbb.59.1786

Substitution of lysine for arginine in the N-terminal 217th amino acid residue of the H gamma II of Staphylococcal gamma-hemolysin lowers the activity of the toxin

Biosci Biotechnol Biochem. 1995 Sep;59(9):1786-9. doi: 10.1271/bbb.59.1786.

Authors

K Sudo¹, W Choorit, I Asami, J Kaneko, K Muramoto, Y Kamio

Affiliation

¹ Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.

PMID: 8520122
DOI: 10.1271/bbb.59.1786

Abstract

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

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Arginine / chemistry*
Bacterial Proteins
Bacterial Toxins / chemistry*
Bacterial Toxins / isolation & purification
Bacterial Toxins / toxicity
Base Sequence
Chromatography / methods
Erythrocytes / drug effects
Hemolysin Proteins / chemistry
Hemolysin Proteins / isolation & purification
Hemolysin Proteins / toxicity
Hemolysis
Humans
Leukocidins / chemistry
Leukocidins / isolation & purification
Leukocidins / toxicity
Lysine / chemistry*
Molecular Sequence Data
Protein Engineering
Structure-Activity Relationship

Substances

Bacterial Proteins
Bacterial Toxins
Hemolysin Proteins
Leukocidins
gamma-hemolysin, Staphylococcus aureus
Arginine
Lysine

Associated data

GENBANK/D42143