Identification of a bacterial inhibitor against g-type lysozyme
| Autor: | J.M. Van Herreweghe, Geert Baggerman, Chris W. Michiels, Kristof Vanoirbeek, Lien Callewaert, Inge W. Nilsen, Paul Declerck, Bjørnar Myrnes, Lise Vanderkelen |
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| Rok vydání: | 2010 |
| Předmět: |
Molecular Sequence Data
medicine.disease_cause Microbiology Cellular and Molecular Neuroscience chemistry.chemical_compound Geese Escherichia coli medicine Animals Amino Acid Sequence Mode of action Molecular Biology DNA Primers Pharmacology Innate immune system biology Escherichia coli Proteins Cell Biology Periplasmic space Surface Plasmon Resonance biology.organism_classification chemistry Biochemistry Chromatography Gel Molecular Medicine Muramidase Peptidoglycan Lysozyme Sequence motif Bacteria |
| Zdroj: | Cellular and Molecular Life Sciences. 68:1053-1064 |
| ISSN: | 1420-9071 1420-682X |
| DOI: | 10.1007/s00018-010-0507-3 |
| Popis: | Lysozymes are antibacterial effectors of the innate immune system in animals that hydrolyze peptidoglycan. Bacteria have evolved protective mechanisms that contribute to lysozyme tolerance such as the production of lysozyme inhibitors, but only inhibitors of chicken (c-) and invertebrate (i-) type lysozyme have been identified. We here report the discovery of a novel Escherichia coli inhibitor specific for goose (g-) type lysozymes, which we designate PliG (periplasmic lysozyme inhibitor of g-type lysozyme). Although it does not inhibit c- or i-type lysozymes, PliG shares a structural sequence motif with the previously described PliI and MliC/PliC lysozyme inhibitor families, suggesting a common ancestry and mode of action. Deletion of pliG increased the sensitivity of E. coli to g-type lysozyme. The existence of inhibitors against all major types of animal lysozyme and their contribution to lysozyme tolerance suggest that lysozyme inhibitors may play a role in bacterial interactions with animal hosts. |
| Databáze: | OpenAIRE |
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