Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria
| Autor: | Frédérique Lembo, Vincent Monchois, Deborah Byrne, Jean-Michel Claverie, Sabine Chenivesse, Jean-Claude Lazzaroni, Chantal Abergel |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Gram-negative bacteria Protein family Protein Conformation medicine.disease_cause Bacterial cell structure Microbiology Evolution Molecular chemistry.chemical_compound Protein structure Species Specificity medicine Cluster Analysis Escherichia coli Phylogeny Crystallography Multidisciplinary biology Escherichia coli Proteins Biological Sciences biology.organism_classification chemistry Biochemistry Muramidase Peptidoglycan Lysozyme Carrier Proteins Bacteria |
| Zdroj: | Proceedings of the National Academy of Sciences. 104:6394-6399 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0611019104 |
| Popis: | Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antilysozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such, Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates. |
| Databáze: | OpenAIRE |
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