Anionic C-terminal proregion of nematode antimicrobial peptide cecropin P4 precursor inhibits antimicrobial activity of the mature peptide.
Recently, an anionic proregion was found to be conserved at the C terminus of the antimicrobial peptide, nematode cecropin. Our results suggest that the antimicrobial activity of mature peptide is suppressed by the proregion in its precursor and is released from inhibition after processing. Inhibition is not likely to be due to direct suppression of membrane disruption.
Ueno
Satoshi
S
Division of Insect Sciences, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.
Kusaka
Kohtaro
K
Tamada
Yasushi
Y
Minaba
Masaomi
M
Zhang
Hong
H
Wang
Pi-Chao
PC
Kato
Yusuke
Y
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000037:antagonists & inhibitors* / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D001419:Bacteria / Q000166:cytology / Q000187:drug effects*; D054807:Cecropins / Q000037:antagonists & inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D008969:Molecular Sequence Data; D009348:Nematoda / Q000737:chemistry*; D011498:Protein Precursors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*
D000890:Anti-Infective Agents; D054807:Cecropins; D011498:Protein Precursors