Antibacterial activity of a novel 26-kDa serine protease in the yellow body of Sarcophaga peregrina (flesh fly) pupae.
We have reported a novel serine protease produced by Sarcophaga peregrina (Nakajima et al., J. Biol. Chem. 272 (1997) 23805-23810). This 26-kDa protease showed antibacterial activity against several bacteria. This activity was an intrinsic characteristic of the enzyme protein and not directly related to its protease activity, because treating the 26-kDa protease with diisopropyl fluorophosphate had no appreciable effect on its antibacterial activity. Unlike bovine trypsin, the 26-kDa protease interacted with acidic phospholipids, suggesting that its antibacterial activity is attributable to interaction with bacterial membranes.
Tsuji
Y
Y
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Nakajima
Y
Y
Homma
K
K
Natori
S
S
D000818:Animals; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000302:isolation & purification / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000187:drug effects; D002175:Candida / Q000187:drug effects; D003352:Corynebacterium / Q000187:drug effects; D004175:Diptera / Q000201:enzymology* / Q000254:growth & development; D004926:Escherichia coli / Q000187:drug effects; D007814:Larva / Q000201:enzymology*; D008675:Metamorphosis, Biological; D008826:Microbial Sensitivity Tests; D012485:Salmonella typhi / Q000187:drug effects; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000187:drug effects
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D012697:Serine Endopeptidases