Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei.

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.

• Authors: Radka Josková, Marcela Silerová, Petra Procházková, Martin Bilej
• Journal: Developmental and comparative immunology (Dev Comp Immunol) Vol. 33 Issue 8 Pg. 932-8 (Aug 2009) ISSN: 1879-0089 [Electronic] United States
• PMID: 19454335 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Muramic Acids
• N-acetylmuramic acid
• N-acetylglucopyranosylamine
• Chitinases
• Muramidase
• Endopeptidases
• fibrin destabilase
• Carbon-Nitrogen Lyases
• isopeptidase
• Glucosamine

Topics

• Animals
• Bacillus subtilis (immunology, pathogenicity)
• Bacterial Adhesion
• Carbon-Nitrogen Lyases (metabolism)
• Chitinases (metabolism)
• Cloning, Molecular
• Echinodermata (genetics)
• Endopeptidases (metabolism)
• Escherichia coli (genetics, immunology, pathogenicity)
• Escherichia coli Infections (immunology)
• Glucosamine (analogs & derivatives, immunology, metabolism)
• Gram-Positive Bacterial Infections (immunology)
• Hirudo medicinalis (genetics)
• Host-Pathogen Interactions
• Hydrolysis
• Muramic Acids (immunology, metabolism)
• Muramidase (genetics, immunology, metabolism)
• Oligochaeta (enzymology, genetics, immunology)
• Sequence Homology
• Virulence