The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm

FEBS Letters

Sandvik, K.¹  Ulvatne, H.¹  Vorland, L.H.¹  Haukland, H.H.¹ 

[1] Department of Medical Microbiology, University Hospital of Tromsø, N-9038 Tromsø, Norway

关键词: Antimicrobial peptide;    Lactoferricin;    Magainin;    Cecropin;    Cytoplasmic membrane;    Cytoplasm;    Lfcin B;    bovine lactoferricin;    Cec P1;    cecropin P1;    Mag 2;    magainin 2;    BPW;    Bacto peptone water;    MIC;    minimal inhibitory concentration;    MBC;    minimal bactericidal concentration;    CFU;    colony-forming units;    TEM;    transmission electron microscopy;   

DOI  :  10.1016/S0014-5793(01)03100-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy. Staphylococcus aureus and Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and D-lactoferricin B (17–31). E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In S. aureus the amount of cytoplasmic lactoferricin B (17–41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of E. coli. The finding of intracellularly localized magainin is not reported previously.

【 授权许可】

Unknown