1993•FEBS LettersOpen access

The two Staphylococcal bi‐component toxins, leukocidin and gamma‐hemolysin, share one component in common

Yoshiyuki Kamio, Md Arifur Rahman, Hirofumi Nariya, Toshiko Ozawa, Kazuo Izaki

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Abstract

Staphylococcal bi-component toxins, leukocidin and gamma-hemolysin, consist of two protein components, i.e. F and S for leukocidin and H gamma I and H gamma II for gamma-hemolysin. In this study we purified H gamma I and H gamma II to homogeneity from the culture medium of Staphylococcus aureus RIMD 310925 and compared their properties with those of F and S purified from the same source. The N-terminal 59- and C-terminal 2-residue amino acid sequences, apparent molecular mass, and isoelectric point of purified H gamma I were the same as those of F. In an Ouchterlony double diffusion test a fused line without spur was formed between F and H gamma I using either anti-F or anti-H gamma I antibodies. A synergistic action of F and H gamma II caused hemolysis of human red blood cells, and H gamma I acted synergistically with S to exhibit leukocidin activity. We conclude that the two toxins share one protein component (F = H gamma I) in common and leukocidin- and gamma-hemolysin-specific activities are determined by S and H gamma II, respectively. It is also reported that the N-terminal 58-residue sequence of H gamma II is 72% similar to the corresponding sequence of S.

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Staphylococcal bi-component toxins, leukocidin and gamma-hemolysin, consist of two protein components, i.e. F and S for leukocidin and H gamma I and H gamma II for gamma-hemolysin. In this study we purified H gamma I and H gamma II to homogeneity from the culture medium of Staphylococcus aureus RIMD 310925 and compared their properties with those of F and S purified from the same source. The N-terminal 59- and C-terminal 2-residue amino acid sequences, apparent molecular mass, and isoelectric point of purified H gamma I were the same as those of F. In an Ouchterlony double diffusion test a fused line without spur was formed between F and H gamma I using either anti-F or anti-H gamma I antibodies. A synergistic action of F and H gamma II caused hemolysis of human red blood cells, and H gamma I acted synergistically with S to exhibit leukocidin activity. We conclude that the two toxins share one protein component (F = H gamma I) in common and leukocidin- and gamma-hemolysin-specific activities are determined by S and H gamma II, respectively. It is also reported that the N-terminal 58-residue sequence of H gamma II is 72% similar to the corresponding sequence of S.

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Available abstract

Staphylococcal bi-component toxins, leukocidin and gamma-hemolysin, consist of two protein components, i.e. F and S for leukocidin and H gamma I and H gamma II for gamma-hemolysin. In this study we purified H gamma I and H gamma II to homogeneity from the culture medium of Staphylococcus aureus RIMD 310925 and compared their properties with those of F and S purified from the same source. The N-terminal 59- and C-terminal 2-residue amino acid sequences, apparent molecular mass, and isoelectric point of purified H gamma I were the same as those of F. In an Ouchterlony double diffusion test a fused line without spur was formed between F and H gamma I using either anti-F or anti-H gamma I antibodies. A synergistic action of F and H gamma II caused hemolysis of human red blood cells, and H gamma I acted synergistically with S to exhibit leukocidin activity. We conclude that the two toxins share one protein component (F = H gamma I) in common and leukocidin- and gamma-hemolysin-specific activities are determined by S and H gamma II, respectively. It is also reported that the N-terminal 58-residue sequence of H gamma II is 72% similar to the corresponding sequence of S.

Key concepts: Hemolysin, Leukocidin, Component (thermodynamics), Microbiology, Staphylococcus aureus, Panton–Valentine leukocidin, Chemistry, Biology

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