Antibacterial activity of a novel 26-kDa serine protease in the yellow body of Sarcophaga peregrina (flesh fly) pupae

FEBS Letters
Y TsujiS Natori

Abstract

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.

References

Jul 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·J E GabayC F Nathan

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Citations

May 29, 2002·Developmental and Comparative Immunology·Daiwu KangHåkan Steiner
Jul 30, 1999·Developmental and Comparative Immunology·S NatoriA Kobayashi
Jan 25, 2006·Insect Biochemistry and Molecular Biology·David M Donnell, Michael R Strand

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