Back to Search
Start Over
A novel peptidoglycan recognition protein containing a goose-type lysozyme domain from the Pacific oyster, Crassostrea gigas
- Source :
-
Molecular Immunology . May2009, Vol. 46 Issue 8/9, p1768-1774. 7p. - Publication Year :
- 2009
-
Abstract
- Abstract: Peptidoglycan recognition protein (PGRP) is considered an essential molecule for effective immunity in invertebrates by its detection and clarification of invading bacteria. Bivalve mollusks also possess PGRP systems for self-defense, however, their functions in bivalves remain to be understood. In the present study, cDNA of a novel PGRP was identified from the Pacific oyster, Crassostrea gigas, using EST-based RACE PCR. This novel PGRP is homologous to short PGRPs and the presence of a signal peptide was predicted. The PGRP is classified into the short PGRP group, although its molecular weight was estimated as 54kDa, close to that of long PGRP groups. A conserved domain search detected amidase_2/PGRP and goose-type (g-type) lysozyme domains in this PGRP structure, and thus this novel PGRP was designated as CgPGRP-L. Catalytic residues for PGRP and g-type lysozyme are well conserved, suggesting that CgPGRP-L may have both binding and lytic functions against bacteria. Reverser transcription PCR (RT-PCR) detected CgPGRP-L mRNA expression in circulatory hemocytes, and quantitative real-time RT-PCR revealed that its expression increased after Marinococcus halophilus and Vibrio tubiashii exposure. These results indicate that CgPGRP-L is expressed in hemocytes by bacterial invasion, and then may play roles of a short PGRP and bacterio-lytic lysozyme. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 01615890
- Volume :
- 46
- Issue :
- 8/9
- Database :
- Academic Search Index
- Journal :
- Molecular Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 37812877
- Full Text :
- https://doi.org/10.1016/j.molimm.2009.01.022