1. In vitro synthesis of the delta-lysin of Staphylococcus aureus
K Y Lee, T H Birkbeck Infect Immun. 1984 May;44(2):434-8. doi: 10.1128/iai.44.2.434-438.1984.
The stability of mRNA for the delta-lysin of Staphylococcus aureus was determined by measuring the residual lysin synthesis after inhibition of DNA-dependent RNA polymerase activity with rifampin. At the late logarithmic-early stationary phase of growth the delta-lysin mRNA was very stable, with a half-life of ca. 20 min. Total cellular RNA was extracted from S. aureus and translated with a modified Escherichia coli S-30 system; delta-lysin was identified amongst the translation products by immunoprecipitation and immunoabsorption. The delta-lysin synthesized in vitro was of a size similar to mature delta-lysin and did not require a signal sequence for secretion from the cell.
2. Characterization of anti-Legionella activity of warnericin RK and delta-lysin I from Staphylococcus warneri
Julien Verdon, Jean-Marc Berjeaud, Christian Lacombe, Yann Héchard Peptides. 2008 Jun;29(6):978-84. doi: 10.1016/j.peptides.2008.01.017. Epub 2008 Feb 6.
Legionella pneumophila, the causative agent of Legionnaires' disease, is a waterborne bacteria. It can multiply in man-made water systems and infect people who inhale contaminated droplets. We have previously reported a Staphylococcus warneri strain that display an anti-Legionella activity. In this work, we characterized three anti-Legionella peptides that are produced by S. warneri. One peptide, warnericin RK, is original, while the two others are delta-lysin I and delta-lysin II, whose genes were previously described. Due to high sequence similarity of the two delta-lysins, further characterization was performed only on delta-lysin I. Warnericin RK and delta-lysin I displayed the same antibacterial spectrum, which is almost restricted to the Legionella genus. Also, both peptides have a hemolytic activity. These results led to the hypothesis that warnericin RK and delta-lysin I share a similar mode of action, and that Legionella should have a specific feature that may explain the high specificity of these antibacterial peptides.
3. Conformation and activity of delta-lysin and its analogs
Vishnu M Dhople, Ramakrishnan Nagaraj Peptides. 2005 Feb;26(2):217-25. doi: 10.1016/j.peptides.2004.09.013.
Delta-Lysin is a 26-residue hemolytic peptide secreted by Staphylococcus aureus. Unlike the bee venom peptide melittin, delta-lysin does not exhibit antibacterial activity. We have synthesized delta-lysin and several analogs wherein the N-terminal residues of the toxin were sequentially deleted. The toxin has three aspartic acids, four lysines and no prolines. Analogs were also generated in which all the aspartic acids were replaced with lysines. A proline residue was introduced in the native sequences as well as in the analogs where aspartic acids were replaced with lysines. We observed that 20- and 22-residue peptides corresponding to residues 7-26 and 5-26 of delta-lysin, respectively, had greater hemolytic activity than the parent peptide. These shorter peptides, unlike delta-lysin, did not self-associate to adopt alpha-helical conformation in water, at lytic concentrations. Introduction of proline or substitution of aspartic acids by lysines resulted in loss in propensity to adopt helical conformation in water. When proline was introduced in the peptides corresponding to the native toxin sequence, loss of hemolytic activity was observed. Substitution of all the aspartic acids with lysines resulted in enhanced hemolytic activity in all the analogs. However, when both proline and aspartic acid to lysine changes were made, only antibacterial activity was observed in the shorter peptides. Our investigations on delta-lysin and its analogs provide insights into the positioning of anionic, cationic residues and proline in determining hemolytic and antibacterial activities.
