Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19454335
DOI
10.1016/j.dci.2009.03.002
PII: S0145-305X(09)00062-7
Knihovny.cz E-resources
- MeSH
- Bacillus subtilis immunology pathogenicity MeSH
- Bacterial Adhesion MeSH
- Chitinases metabolism MeSH
- Echinodermata genetics MeSH
- Endopeptidases metabolism MeSH
- Escherichia coli genetics immunology pathogenicity MeSH
- Glucosamine analogs & derivatives immunology metabolism MeSH
- Gram-Positive Bacterial Infections immunology MeSH
- Hydrolysis MeSH
- Escherichia coli Infections immunology MeSH
- Host-Pathogen Interactions MeSH
- Cloning, Molecular MeSH
- Muramic Acids immunology metabolism MeSH
- Carbon-Nitrogen Lyases metabolism MeSH
- Muramidase genetics immunology metabolism MeSH
- Oligochaeta enzymology genetics immunology MeSH
- Hirudo medicinalis genetics MeSH
- Sequence Homology MeSH
- Virulence MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Chitinases MeSH
- Endopeptidases MeSH
- fibrin destabilase MeSH Browser
- Glucosamine MeSH
- isopeptidase MeSH Browser
- Muramic Acids MeSH
- Carbon-Nitrogen Lyases MeSH
- Muramidase MeSH
- N-acetylglucopyranosylamine MeSH Browser
- N-acetylmuramic acid MeSH Browser
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.
References provided by Crossref.org
Contribution of Eisenia andrei earthworms in pathogen reduction during vermicomposting
