Abstract
Lysozyme is a widely distributed antimicrobial protein having specificity for cleaving the beta-(1,4)-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (GlcNAc) of peptidoglycan of the bacterial cell walls and thus efficiently contributes to protection against infections caused mainly by Gram-positive bacteria. In the present study, we assembled a full-length cDNA of a novel invertebrate-type lysozyme from Eisenia andrei earthworm (EALys) by RT-PCR and RACE system. The primary structure of EALys shares high homology with other invertebrate lysozymes; however the highest, 72% identity, was shown for the destabilase I isolated from medicinal leech. Recombinant EALys expressed in Escherichia coli exhibited the lysozyme and isopeptidase activity. Moreover, real-time PCR revealed increased levels of lysozyme mRNA in coelomocytes of E. andrei after the challenge with both Gram-positive and Gram-negative bacteria.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Bacillus subtilis / immunology*
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Bacillus subtilis / pathogenicity
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Bacterial Adhesion
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Carbon-Nitrogen Lyases / metabolism
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Chitinases / metabolism
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Cloning, Molecular
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Echinodermata / genetics
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Endopeptidases / metabolism
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Escherichia coli / genetics
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Escherichia coli / immunology*
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Escherichia coli / pathogenicity
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Escherichia coli Infections / immunology
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Glucosamine / analogs & derivatives
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Glucosamine / immunology
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Glucosamine / metabolism
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Gram-Positive Bacterial Infections / immunology
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Hirudo medicinalis / genetics
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Host-Pathogen Interactions
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Hydrolysis
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Muramic Acids / immunology
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Muramic Acids / metabolism
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Muramidase / genetics*
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Muramidase / immunology
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Muramidase / metabolism
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Oligochaeta / enzymology*
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Oligochaeta / genetics*
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Oligochaeta / immunology
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Sequence Homology
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Virulence
Substances
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Muramic Acids
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N-acetylmuramic acid
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N-acetylglucopyranosylamine
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Chitinases
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Muramidase
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Endopeptidases
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fibrin destabilase
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Carbon-Nitrogen Lyases
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isopeptidase
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Glucosamine