Antinematodal effect of antimicrobial peptide, PMAP-23, isolated from porcine myeloid against Caenorhabditis elegans.
The antinematodal activity and mechanism of a 23-mer antimicrobial peptide, PMAP-23, derived from pig myeloid was investigated. PMAP-23 displayed a strong antinematodal activity against the eggs and worms of Caenorhabditis elegans. To investigate the antinematodal mechanism of PMAP-23, fluorescence activated flow cytometry and confocal laser scanning microscopy were performed. C. elegans treated with PMAP-23 showed higher fluorescence intensity by propidium iodide (PI) staining than normal cells. Confocal microscopy showed that the peptide was localized in the egg's shell and cell membrane. The action of the peptide against C. elegans membranes was examined by testing the membrane disrupting activity using liposome (PC/PS; 3:1, w/w). The result suggests that PMAP-23 may exert its antinematodal activity by disrupting the structure of the cell membrane via pore formation or via direct interaction with the lipid bilayers.
Park
Yoonkyung
Y
Research Center for Proteineous Materials, Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, Republic of Korea.
Jang
Seung-Hwan
SH
Lee
Dong Gun
DG
Hahm
Kyung-Soo
KS
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D000969:Antinematodal Agents / Q000494:pharmacology*; D017173:Caenorhabditis elegans / Q000187:drug effects* / Q000254:growth & development; D002462:Cell Membrane / Q000187:drug effects*; D004531:Eggs; D008051:Lipid Bilayers; D013552:Swine
D023181:Antimicrobial Cationic Peptides; D000969:Antinematodal Agents; D008051:Lipid Bilayers; C086301:porcine myeloid antibacterial peptide 23