[3] Purification and assay of staphylococcal δ-lysin

Birkbeck, T. H.; Freer, John H.

doi:10.1016/s0076-6879(88)65006-3

Cited by 16 publications

(12 citation statements)

References 13 publications

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“…We demonstrated that our purified fraction (Fraction III) possessed hemolytic activity on horse erythrocytes. The hemolytic activity was 790 units/mg protein, which is consistent with that in a previous report (310 units/mg protein) (25). To confirm the inhibitory activity of ␦-hemolysin against colony spreading, we examined whether chemically synthesized ␦-hemolysin inhibits colony spreading.…”

Section: S Aureus Secretes Inhibitors Against Colonysupporting

confidence: 89%

“…The sequence was matched with amino acid residues of ␦-hemolysin (Hld, ␦-toxin), which is encoded by the hld gene in the agr locus (24). ␦-Hemolysin is reported to have hemolytic activity on horse erythrocytes (25). We demonstrated that our purified fraction (Fraction III) possessed hemolytic activity on horse erythrocytes.…”

Section: S Aureus Secretes Inhibitors Against Colonymentioning

confidence: 91%

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Inhibition of Colony-spreading Activity of Staphylococcus aureus by Secretion of δ-Hemolysin

Omae

Sekimizu

Kaito

2012

Journal of Biological Chemistry

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Section: S Aureus Secretes Inhibitors Against Colonysupporting

confidence: 89%

Section: S Aureus Secretes Inhibitors Against Colonymentioning

confidence: 91%

Inhibition of Colony-spreading Activity of Staphylococcus aureus by Secretion of δ-Hemolysin

Omae

Sekimizu

Kaito

2012

Journal of Biological Chemistry

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“…Hlg/Luk and α‐hemolysin (Hla) were detected by Western immunoblotting using specific antisera raised against Hlg2, LukF and LukS for Hlg/Luk, and anti‐Hla antiserum, respectively (Kaneko et al , 1997). For the assay of δ‐hemolysin (Hld) production, 20 μL of culture supernatant was incubated at 60°C for 10 min and placed into a sample well on a human red blood cell agarose plate (Birkbeck & Freer, 1988). Under these conditions, Hld still retains its activity, whereas Hlg loses its activity.…”

Section: Methodsmentioning

confidence: 99%

Expression of Î³-hemolysin regulated bysaeinStaphylococcus aureusstrain Smith 5R

Yamazaki

Kato

Kamio

et al. 2006

FEMS Microbiology Letters

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Staphylococcus aureus strain Smith 5R produces a two-component pore-forming toxin and forms a rough-surfaced colony with hemolytic haloes on human red blood cell plates (R[+]). Serial subcultures of the strain in broth caused the appearance of gamma-hemolysin negative variants with a smooth colony shape (S[-]), and the S[-] valiant became predominant in culture. The R[+] strain, in which agrA is naturally disrupted by an insertion of IS1181, produced high levels of gamma-hemolysin. In the S[-] variant, expression of both hlg and lukS-F mRNAs was strongly reduced. Nucleotide sequencing of the sae locus revealed that all isolated S[-] variants had spontaneous mutations in the sae locus. Recovery of gamma-hemolysin productivity in S[-] by transformation of the wild-type sae allele strongly suggested that the expression of gamma-hemolysin is positively regulated by sae in an agr-independent manner.

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“…Formyl-NH-Met-Ala-Gln-Asp-Ile-Ile-Ser-Thr-Ile-Gly-Asp-Leu-Val-Lys-Trp-Ile-Ile-Asp-Thr-Val-Asn-Lys-Phe-Thr-Lys-Lys-COOH (d-Lysin) was a gift from Dr. Birkbeck (University of Glasgow, Scotland). Its purification was described previously (1,44). For the dye efflux kinetics measurements, lyophilized d-lysin was dissolved in distilled water acidified to pH ' 3, to a final concentration of 200 mM as described before (3).…”

Section: D-lysinmentioning

confidence: 99%

Temperature and Composition Dependence of the Interaction of δ-Lysin with Ternary Mixtures of Sphingomyelin/Cholesterol/POPC

Pokorny

Yandek

Elegbede

et al. 2006

Biophysical Journal

144

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The kinetics of carboxyfluorescein efflux induced by the amphipathic peptide delta-lysin from vesicles of porcine brain sphingomyelin (BSM), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and cholesterol (Chol) were investigated as a function of temperature and composition. Sphingomyelin (SM)/Chol mixtures form a liquid-ordered (L(o)) phase whereas POPC exists in the liquid-disordered (L(d)) phase at ambient temperature. delta-Lysin binds strongly to L(d) and poorly to L(o) phase. In BSM/Chol/POPC vesicles the rate of carboxyfluorescein efflux induced by delta-lysin increases as the POPC content decreases. This is explained by the increase of delta-lysin concentration in L(d) domains, which enhances membrane perturbation by the peptide. Phase separations in the micrometer scale have been observed by fluorescence microscopy in SM/Chol/POPC mixtures for some SM, though not for BSM. Thus, delta-lysin must detect heterogeneities (domains) in BSM/Chol/POPC on a much smaller scale. Advantage was taken of the inverse variation of the efflux rate with the L(d) content of BSM/Chol/POPC vesicles to estimate the L(d) fraction in those mixtures. These results were combined with differential scanning calorimetry to obtain the BSM/Chol/POPC phase diagram as a function of temperature.

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[3] Purification and assay of staphylococcal δ-lysin

Cited by 16 publications

References 13 publications

Inhibition of Colony-spreading Activity of Staphylococcus aureus by Secretion of δ-Hemolysin

Inhibition of Colony-spreading Activity of Staphylococcus aureus by Secretion of δ-Hemolysin

Expression of Î³-hemolysin regulated bysaeinStaphylococcus aureusstrain Smith 5R

Temperature and Composition Dependence of the Interaction of δ-Lysin with Ternary Mixtures of Sphingomyelin/Cholesterol/POPC

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