Antinematodal activity and the mechanism of the antimicrobial peptide, HP (2-20), against Caenorhabditis elegans.
The peptide HP (2-20), derived from the N-terminal sequence of Helicobacter pylori ribosomal protein L1 (RPL1), has a nematicidal activity against eggs and worms of Caenorhabditis elegans. Eggs treated with HP (2-20) (69%) has a higher fluorescence intensity with propidium iodide staining, which was similar to that of melittin (82%) but higher than untreated cells (5.7%). Confocal microscopy showed that the peptides were located in the shell of the eggs and the inner and outer surfaces of the worms. HP (2-20) therefore may exert its antinematodal activity by disrupting the structure of the egg's shell and the cell membrane via pore formation or by direct interaction with the lipid bilayers in a detergent-like manner.
Jang
Seung-Hwan
SH
Research Center for Proteineous Materials, Chosun University, 375 Seosuk-Dong, Dong-Ku, Kwangju 501-759, Korea.
Park
Yoonkyung
Y
Park
Seong-Cheol
SC
Kim
Pyoung Il
PI
Lee
Dong Gun
DG
Hahm
Kyung-Soo
KS
D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology; D000969:Antinematodal Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000494:pharmacology*; D017173:Caenorhabditis elegans; D003902:Detergents / Q000494:pharmacology; D005434:Flow Cytometry; D016480:Helicobacter pylori / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry; D008555:Melitten / Q000494:pharmacology; D018613:Microscopy, Confocal; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D011419:Propidium / Q000494:pharmacology
D000890:Anti-Infective Agents; D000969:Antinematodal Agents; D001426:Bacterial Proteins; D003902:Detergents; C433783:Hp (2-20) protein, Helicobacter pylori; D008051:Lipid Bilayers; D010446:Peptide Fragments; D010455:Peptides; D008555:Melitten; D011419:Propidium