Molecular characterisation, evolution and expression analysis of g-type lysozymes in Ciona intestinalis.
Lysozyme is an important defense molecule of the innate immune system. Known for its bactericidal properties, lysozyme catalyzes the hydrolysis of b-(1,4)-glycosidic bonds between the N-acetyl glucosamine and N-acetyl muramic acid in the peptidoglycan layer of bacterial cell walls. In this study, the complete coding sequence of four g-type lysozymes were identified in Ciona intestinalis. Phylogenetic analysis and modelling supported the hypothesis of a close relationship with the vertebrate g-type lysozymes suggesting that the C. intestinalis g-type lysozyme genes (CiLys-g1, Cilys-g2, CiLys-g3, CiLys-g4) share a common ancestor in the chordate lineage. Protein motif searches indicated that C. intestinalis g-type lysozymes contain a GEWL domain with a GXXQ signature, typical of goose lysozymes. Quantitative Real-Time PCR analysis results showed that transcripts are expressed in various tissues from C. intestinalis. In order to determine the involvement of C. intestinalis g-type lysozymes in immunity, their expression was analyzed in the pharynx, showing that transcripts were significantly up-regulated in response to a challenge with lipopolysaccharide (LPS). These data support the view that CiLys g-type are molecules with potential for immune defense system against bacterial infection.
Marine Immunobiology Laboratory, Department of Biological, Chemical, Pharmaceutical Science and Technology, University of Palermo, Via Archirafi 18, Palermo, Italy.
Felicia
F
Di Falco
Marine Immunobiology Laboratory, Department of Biological, Chemical, Pharmaceutical Science and Technology, University of Palermo, Via Archirafi 18, Palermo, Italy.
Matteo
M
Cammarata
Marine Immunobiology Laboratory, Department of Biological, Chemical, Pharmaceutical Science and Technology, University of Palermo, Via Archirafi 18, Palermo, Italy. Electronic address: aiti.vizzini@unipa.it.
Aiti
A
Vizzini
D000818:Animals; D001424:Bacterial Infections / Q000276:immunology*; D001433:Bacteriolysis; D005075:Biological Evolution; D002478:Cells, Cultured; D002938:Ciona intestinalis / Q000276:immunology*; D003001:Cloning, Molecular; D019143:Evolution, Molecular; D005777:Geese / Q000276:immunology; D007113:Immunity, Innate; D008070:Lipopolysaccharides / Q000276:immunology; D009113:Muramidase / Q000235:genetics / Q000378:metabolism*; D010614:Pharynx / Q000378:metabolism*; D010802:Phylogeny; D059467:Transcriptome
D008070:Lipopolysaccharides; D009113:Muramidase
Ascidian; Ciona intestinalis; Inflammation; LPS; Lysozymes g-type