TY - JOUR
T1 - Oyster hemocytes express a proline-rich peptide displaying synergistic antimicrobial activity with a defensin
AU - Gueguen, Yannick
AU - Bernard, Romestand
AU - Julie, Fievet
AU - Paulina, Schmitt
AU - Delphine, Destoumieux Garzón
AU - Franck, Vandenbulcke
AU - Philippe, Bulet
AU - Evelyne, Bachère
N1 - Funding Information:
This study was part of a collaborative project supported by the European Commission, DG XII, in the program International Cooperation with Developing Countries, INCO-DC, Contract no. ICA4-CT-2001-10023 (IMMUNAQUA). The work was also funded by the CNRS (Centre National de la Recherche Scientifique), the Ifremer and the University of Montpellier 2. We are very grateful to Dr. L. Otvos for helpful discussion, Dr. D. Flament for assistance in bioinformatics analyses and M. Leroy for technical assistance.
PY - 2009/2
Y1 - 2009/2
N2 - A cDNA sequence that encodes a 61-amino acid polypeptide precursor with homologies to proline-rich antimicrobial peptides (AMPs) was identified in the oyster Crassostrea gigas. After release of a hydrophobic signal peptide, the resulting 37-amino acid peptide, Cg-Prp, is composed of an acidic region and a cationic proline-rich region. To evaluate the biological properties of Cg-Prp, multiple proline-rich peptides corresponding to putative processing of the full-length Cg-Prp were synthesized. A limited antimicrobial activity was observed for two of them, which also showed strong synergistic antimicrobial activity with Cg-Def, a defensin from C. gigas. To our knowledge, this is the first evidence of synergy between a defensin and another AMP in an invertebrate. By in situ hybridization, the expression of Cg-prp was found to be restricted to hemocytes and induced following bacterial challenge. Cg-prp transcripts were also detected in hemocytes infiltrating mantle, where Cg-Def is expressed. Additionally, by immunocytochemistry, we showed that Cg-Prp or one of its variants is present in some hemocytes together with defensins. In conclusion, we described here the first proline-rich AMP from mollusk. From our study, it is likely to provide a first line of defense against bacterial invasion by acting through synergy with defensins.
AB - A cDNA sequence that encodes a 61-amino acid polypeptide precursor with homologies to proline-rich antimicrobial peptides (AMPs) was identified in the oyster Crassostrea gigas. After release of a hydrophobic signal peptide, the resulting 37-amino acid peptide, Cg-Prp, is composed of an acidic region and a cationic proline-rich region. To evaluate the biological properties of Cg-Prp, multiple proline-rich peptides corresponding to putative processing of the full-length Cg-Prp were synthesized. A limited antimicrobial activity was observed for two of them, which also showed strong synergistic antimicrobial activity with Cg-Def, a defensin from C. gigas. To our knowledge, this is the first evidence of synergy between a defensin and another AMP in an invertebrate. By in situ hybridization, the expression of Cg-prp was found to be restricted to hemocytes and induced following bacterial challenge. Cg-prp transcripts were also detected in hemocytes infiltrating mantle, where Cg-Def is expressed. Additionally, by immunocytochemistry, we showed that Cg-Prp or one of its variants is present in some hemocytes together with defensins. In conclusion, we described here the first proline-rich AMP from mollusk. From our study, it is likely to provide a first line of defense against bacterial invasion by acting through synergy with defensins.
KW - Antimicrobial peptide
KW - Innate immunity
KW - Invertebrate
KW - Mollusk
KW - Pacific oyster
KW - Synergy
UR - http://www.scopus.com/inward/record.url?scp=58249105860&partnerID=8YFLogxK
U2 - 10.1016/j.molimm.2008.07.021
DO - 10.1016/j.molimm.2008.07.021
M3 - Article
C2 - 18962895
AN - SCOPUS:58249105860
SN - 0161-5890
VL - 46
SP - 516
EP - 522
JO - Molecular Immunology
JF - Molecular Immunology
IS - 4
ER -