The non-enzymatic microbicidal activity of lysozymes
| Autor: | Andreas Mahn, Petra Porsch, Klaus Düring, Werner Gieffers, Olaf Brinkmann |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Phytophthora
Recombinant Fusion Proteins Lysozyme Amphipathic helix Biophysics Biochemistry Microbiology chemistry.chemical_compound Anti-Infective Agents Egg White Structural Biology Escherichia coli Genetics medicine Animals Bacteriophage T4 Molecular Biology Muramidase chemistry.chemical_classification biology Cell Membrane Chitinases Cell Biology Protein engineering medicine.disease Antimicrobial biology.organism_classification Hemolysis Anti-Bacterial Agents Enzyme chemistry Mutagenesis Membrane disturbing activity Peptides Antimicrobial peptide Non-enzymatic microbicidal activity Bacteria Egg white |
| Zdroj: | FEBS Letters. 449:93-100 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(99)00405-6 |
| Popis: | T4 lysozyme was thought to destroy bacteria by its muramidase activity. However, we demonstrate here that amphipathic helix stretches in the C-terminus of T4 lysozyme mediate its bactericidal and fungistatic activities. In heat-denatured T4 lysozyme, the enzymatic activity is completely abolished but unexpectedly, the antimicrobial functions remain preserved. Small synthetic peptides corresponding to amphipathic C-terminal domains of T4 lysozyme show a microbicidal activity. Its membrane disturbing activity was directly demonstrated for bacterial, fungal and plant cells but not in a hemolysis assay. Comparable results were obtained with hen egg white lysozyme. This opens up many new opportunities for optimization of lysozymes as antimicrobial agents in various applications by protein engineering. |
| Databáze: | OpenAIRE |
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