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The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
Author(s) -
Haukland H.H.,
Ulvatne H.,
Sandvik K.,
Vorland L.H.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03100-3
Subject(s) - magainin , cytoplasm , antimicrobial peptides , escherichia coli , staphylococcus aureus , chemistry , microbiology and biotechnology , bacterial cell structure , peptide , antimicrobial , bacteria , biology , biochemistry , genetics , gene
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.