Purification and characterization of a novel delta-lysin variant that inhibits Staphylococcus aureus and has limited hemolytic activity
Delta-lysins (DL) that are produced by various species of staphylococci are not widely known for their antimicrobial activity. We have purified and characterized a novel DL variant, E229DL and examined its spectrum of inhibitory activity. The biological activity of E229DL, produced by Staphylococcus...
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Published in | Peptides (New York, N.Y. : 1980) Vol. 31; no. 9; pp. 1661 - 1668 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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01.09.2010
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Abstract | Delta-lysins (DL) that are produced by various species of staphylococci are not widely known for their antimicrobial activity. We have purified and characterized a novel DL variant, E229DL and examined its spectrum of inhibitory activity. The biological activity of E229DL, produced by
Staphylococcus epidermidis strain E229, shows relatively broad-spectrum activity against Gram-positive pathogens, including representatives of MRSA and epidemic MRSA type 15. E229DL was purified to homogeneity from 95% acidified-methanol extracts of cell cultures by using a series of reversed-phase chromatographic separations. The fully processed form of E229DL is a 25-amino-acid peptide with a predicted mass of 2841.4
Da, but the purified biologically active molecule appears to be N-formylated (mass 2867.33
Da). The DL gene (hld) resembles that of other types of DL, but differs in five codons with hld in
Staphylococcus aureus (26 residues) and one codon with the closest homolog, the
hld-II in
S. warneri (25 residues). The characterization of E229DL showed that its activity is stable in agar exposed to high temperatures (80
°C/45
min). In addition, biological testing of the native and synthetic peptides against a range of human and animal erythrocytes and Vero cells indicated that E229DL is an antibacterial agent with no detectable cytopathic effects at concentrations equivalent to the minimum inhibitory concentration for EMRSA15-A208. Initial investigation of the mode of action of E229DL indicated that it is rapidly lytic for target cells. This is the first description of a native form of DL having only limited cytotoxic activity for eukaryotic cells at concentrations that are inhibitory to staphylococci. |
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AbstractList | Delta-lysins (DL) that are produced by various species of staphylococci are not widely known for their antimicrobial activity. We have purified and characterized a novel DL variant, E229DL and examined its spectrum of inhibitory activity. The biological activity of E229DL, produced by Staphylococcus epidermidis strain E229, shows relatively broad-spectrum activity against Gram-positive pathogens, including representatives of MRSA and epidemic MRSA type 15. E229DL was purified to homogeneity from 95% acidified-methanol extracts of cell cultures by using a series of reversed-phase chromatographic separations. The fully processed form of E229DL is a 25-amino-acid peptide with a predicted mass of 2841.4 Da, but the purified biologically active molecule appears to be N-formylated (mass 2867.33 Da). The DL gene (hld) resembles that of other types of DL, but differs in five codons with hld in Staphylococcus aureus (26 residues) and one codon with the closest homolog, the hld-II in S. warneri (25 residues). The characterization of E229DL showed that its activity is stable in agar exposed to high temperatures (80 degrees C/45 min). In addition, biological testing of the native and synthetic peptides against a range of human and animal erythrocytes and Vero cells indicated that E229DL is an antibacterial agent with no detectable cytopathic effects at concentrations equivalent to the minimum inhibitory concentration for EMRSA15-A208. Initial investigation of the mode of action of E229DL indicated that it is rapidly lytic for target cells. This is the first description of a native form of DL having only limited cytotoxic activity for eukaryotic cells at concentrations that are inhibitory to staphylococci. Delta-lysins (DL) that are produced by various species of staphylococci are not widely known for their antimicrobial activity. We have purified and characterized a novel DL variant, E229DL and examined its spectrum of inhibitory activity. The biological activity of E229DL, produced by Staphylococcus epidermidis strain E229, shows relatively broad-spectrum activity against Gram-positive pathogens, including representatives of MRSA and epidemic MRSA type 15. E229DL was purified to homogeneity from 95% acidified-methanol extracts of cell cultures by using a series of reversed-phase chromatographic separations. The fully processed form of E229DL is a 25-amino-acid peptide with a predicted mass of 2841.4 Da, but the purified biologically active molecule appears to be N-formylated (mass 2867.33 Da). The DL gene (hld) resembles that of other types of DL, but differs in five codons with hld in Staphylococcus aureus (26 residues) and one codon with the closest homolog, the hld-II in S. warneri (25 residues). The characterization of E229DL showed that its activity is stable in agar exposed to high temperatures (80 °C/45 min). In addition, biological testing of the native and synthetic peptides against a range of human and animal erythrocytes and Vero cells indicated that E229DL is an antibacterial agent with no detectable cytopathic effects at concentrations equivalent to the minimum inhibitory concentration for EMRSA15-A208. Initial investigation of the mode of action of E229DL indicated that it is rapidly lytic for target cells. This is the first description of a native form of DL having only limited cytotoxic activity for eukaryotic cells at concentrations that are inhibitory to staphylococci. |
Author | Al-Mahrous, Mohammed Sandiford, Stephanie K. Upton, Mathew Tagg, John R. |
Author_xml | – sequence: 1 givenname: Mohammed surname: Al-Mahrous fullname: Al-Mahrous, Mohammed organization: Medical Microbiology, School of Translational Medicine, University of Manchester, Clinical Sciences Building, Manchester Royal Infirmary, Oxford Road, Manchester, M13 9WL, UK – sequence: 2 givenname: Stephanie K. surname: Sandiford fullname: Sandiford, Stephanie K. organization: Medical Microbiology, School of Translational Medicine, University of Manchester, Clinical Sciences Building, Manchester Royal Infirmary, Oxford Road, Manchester, M13 9WL, UK – sequence: 3 givenname: John R. surname: Tagg fullname: Tagg, John R. organization: Department of Microbiology and Immunology, University of Otago, PO Box 56, Dunedin, New Zealand – sequence: 4 givenname: Mathew surname: Upton fullname: Upton, Mathew email: m.upton@manchester.ac.uk organization: Medical Microbiology, School of Translational Medicine, University of Manchester, Clinical Sciences Building, Manchester Royal Infirmary, Oxford Road, Manchester, M13 9WL, UK |
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Keywords | Delta-lysin (DL) Antibacterial peptides MRSA Coagulase-negative staphylococci Characterization Variant Purification Peptides Antibacterial agent |
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Snippet | Delta-lysins (DL) that are produced by various species of staphylococci are not widely known for their antimicrobial activity. We have purified and... |
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SubjectTerms | Amino Acid Sequence Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - isolation & purification Anti-Bacterial Agents - pharmacology Antibacterial peptides Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - pharmacology Biological and medical sciences Cercopithecus aethiops Coagulase-negative staphylococci Delta-lysin (DL) Fundamental and applied biological sciences. Psychology Gram-Negative Bacteria - drug effects Gram-Positive Bacteria - drug effects Hemolysin Proteins - chemistry Hemolysin Proteins - genetics Hemolysin Proteins - isolation & purification Hemolysin Proteins - pharmacology Hemolysis Hemolytic Agents - chemistry Hemolytic Agents - isolation & purification Hemolytic Agents - pharmacology Hot Temperature Humans Molecular Sequence Data Molecular Weight MRSA Osmolar Concentration Peptides - chemistry Peptides - genetics Peptides - isolation & purification Peptides - pharmacology Protein Processing, Post-Translational Protein Stability Sequence Alignment Staphylococcus aureus - drug effects Staphylococcus aureus - genetics Staphylococcus epidermidis - genetics Staphylococcus epidermidis - metabolism Vero Cells Vertebrates: endocrinology |
Title | Purification and characterization of a novel delta-lysin variant that inhibits Staphylococcus aureus and has limited hemolytic activity |
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