Lysis of Staphylococcus aureus by culture supernatant fluids of a species of Aeromonas

Coles, N. W.; Gilbo, C. M.

doi:10.1128/jb.93.3.1193-1194.1967

Cited by 6 publications

(1 citation statement)

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“…Lytic activity. Lytic factor from the culture supernatant fluid of a species of Aeromonias (2), grown in 2% yeast extract (Difco), was purified and concentrated 20to 25-fold to give a solution containing 45,000 units per ml, as previously defined (2) mately one-quarter of that with whole cells. Lysis.…”

Section: Methodsmentioning

confidence: 99%

Electron Microscopy of the Lysis ofStaphylococcus aureusCell Walls byAeromonasLytic Factor

1967

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Isolated and purified cell walls of Staphylococcus aureus were treated with a purified fraction of the culture supernatant fluid of a species of Aeromonas . The course of lysis of the cell walls was followed over a period of time by examination of samples under an electron microscope. The undifferentiated cell wall was rapidly digested, but the equatorial rings were more resistant. The undifferentiated cell wall became a very thin sheet before completely dissolving, leaving a series of equatorial rings of various widths. As digestion proceeded, solubilization of the entire cell wall occurred. Analogous findings were obtained with purified S. aureus mucopeptide. It is concluded that the Aeromonas lytic principle is an enzyme, and that susceptible bonds are more concentrated in the undifferentiated cell wall mucopeptide.

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Section: Methodsmentioning

confidence: 99%

Electron Microscopy of the Lysis ofStaphylococcus aureusCell Walls byAeromonasLytic Factor

1967

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Aeromonas toxins

Ljungh

Wadström

1981

Pharmacology & Therapeutics

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Purification, properties and mechanism of action of a staphylolytic enzyme produced by Aeromonas hydrophila

Coles

Gilbo

Broad

1969

Biochemical Journal

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1. An enzyme produced by Aeromonas hydrophila and capable of lysing Staphylococcus aureus cells was purified 180-fold by gel filtration and chromatography on columns of AG-50 W resin. 2. Physical measurements on the purified enzyme suggest that it is a small basic protein with an isoelectric point between pH9.0 and pH9.5. 3. Maximum lytic activity was obtained in 20mm-tris-glycine buffer, pH8.5, at 45 degrees , with no detectable activity in the absence of a nitrogenous base. 4. The enzyme is active in the above buffer containing 1.5m-sucrose, and is useful for the preparation of protoplasts of Staphylococcus aureus. 5. Purified cell wall peptidoglycans of two strains of Staphylococcus aureus, differing in amino acid composition, were hydrolysed by the enzyme with the liberation of glycine oligopeptides, principally diglycine and triglycine. 6. Synthetic glycine oligopeptides larger than triglycine, but not polyglycine, were hydrolysed, as were a number of leucine-containing dipeptides and tripeptides, but no proteolytic activity could be demonstrated. 7. It is concluded that the enzyme is lytic towards Staphylococcus aureus because it splits the pentaglycine cross-links of the cell-wall peptidoglycan.

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Lysis of Staphylococcus aureus by culture supernatant fluids of a species of Aeromonas

Cited by 6 publications

References 0 publications

Electron Microscopy of the Lysis ofStaphylococcus aureusCell Walls byAeromonasLytic Factor

Electron Microscopy of the Lysis ofStaphylococcus aureusCell Walls byAeromonasLytic Factor

Aeromonas toxins

Purification, properties and mechanism of action of a staphylolytic enzyme produced by Aeromonas hydrophila

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