MODE OF ACTION OF SAPECIN, A NOVEL ANTIBACTERIAL PROTEIN OF SARCOPHAGA-PEREGRINA (FLESH FLY)

被引:53
作者
MATSUYAMA, K [1 ]
NATORI, S [1 ]
机构
[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123151
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Sapecin is an antibacterial protein purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina [Matsuyama, K. & Natori, S. (1988) J. Biol. Chem 236, 17112-17116]. As this protein inhibited the growth of Gram-positive bacteria better than that of Gram-negative bacteria, we studied its mode of action with special reference to its effects on S. aureus and Escherichia coli. Results showed that sapecin had high affinity for cardiolipin, which is a major phospholipid of S. aureus. Moreover, a mutant of E. coli with a defect in cardiolipin synthesis was more resistant to sapecin than wild type E. coli, suggesting that cardiolipin is a target for sapecin. Lipopolysaccharide of E. coli was also found to be a barrier for the antibacterial activity of sapecin. © 1990 Copyright, 1990 by the Journal of Biochemistry.
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页码:128 / 132
页数:5
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