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Hilde Ulvatne, H. Haukland, Ø. Olsvik, L. Vorland (2001)
Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomesFEBS Letters, 492
D. Wade, A. Boman, B. Wåhlin, C. Drain, D. Andreu, H. Boman, R. Merrifield (1990)
All-D amino acid-containing channel-forming antibiotic peptides.Proceedings of the National Academy of Sciences of the United States of America, 87
H. Boman, B. Agerberth, A. Boman (1993)
Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestineInfection and Immunity, 61
W. Shafer, X. Qu, A. Waring, R. Lehrer (1998)
Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family.Proceedings of the National Academy of Sciences of the United States of America, 95 4
W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase, M. Tomita (1992)
Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin.The Journal of applied bacteriology, 73 6
L. Vorland, Hilde Ulvatne, Ø. Rekdal, J. Svendsen (1999)
Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli.Scandinavian journal of infectious diseases, 31 5
C. Park, Kwan-Su Yi, K. Matsuzaki, Mi Kim, S. Kim (2000)
Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II.Proceedings of the National Academy of Sciences of the United States of America, 97 15
(1993)
Infect. Immun
O. Aguilera, H. Ostolaza, L. Quirós, J. Fierro (1999)
Permeabilizing action of an antimicrobial lactoferricin‐derived peptide on bacterial and artificial membranesFEBS Letters, 462
William Heller, Alan Waring, Robert Lehrer, T. Harroun, Thomas Weiss, Lin Yang, Huey Huang (2000)
Membrane thinning effect of the beta-sheet antimicrobial protegrin.Biochemistry, 39 1
M. Tomita, W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase (1991)
Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin.Journal of dairy science, 74 12
Jong-Youn Lee, A. Boman, Chuanxin Sun, Mats AnderssonT, H. Jornvall, Viktor MUTTt, H. Boman (1989)
Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.Proceedings of the National Academy of Sciences of the United States of America, 86 23
Hilde Ulvatne, L. Vorland (2001)
Bactericidal kinetics of 3 lactoferricins against Staphylococcus aureus and Escherichia coli.Scandinavian journal of infectious diseases, 33 7
M. Zasloff (1987)
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursorProceedings of the National Academy of Sciences of the United States of America, 84
L. Vorland, Hilde Ulvatne, J. Andersen, H. Haukland, Ø. Rekdal, J. Svendsen, T. Gutteberg (1998)
Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin.Scandinavian journal of infectious diseases, 30 5
C. Park, Hun Kim, S. Kim (1998)
Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions.Biochemical and biophysical research communications, 244 1
R. Bessalle, Aviva Kapitkovsky, Alfred Gorea, Itamar Shalit, Mati Fridkin (1990)
All‐D‐magainin: chirality, antimicrobial activity and proteolytic resistanceFEBS Letters, 274
E. Gazit, A. Boman, H. Boman, Y. Shai (1995)
Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles.Biochemistry, 34 36
Hancock (1999)
10.1128/AAC.43.6.1317Antimicrob. Agents Chemother., 43
Hancock (1997)
10.1016/S0140-6736(97)80051-7Lancet, 349
Manhong Wu, E. Maier, R. Benz, R. Hancock (1999)
Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli.Biochemistry, 38 22
C. Subbalakshmi, N. Sitaram (1998)
Mechanism of antimicrobial action of indolicidin.FEMS microbiology letters, 160 1
L. Vorland, Hilde Ulvatne, Johan Andersen, H. Haukland, Ø. Rekdal, J. Svendsen, Tore Gutteberg (1999)
Antibacterial effects of lactoferricin B.Scandinavian journal of infectious diseases, 31 2
(2000)
TEM of E. coli. The cells are exposed to MIC of Cec P1 for 30 min (a) and 2 h (b). Cec P1 is visualized with gold-marked antibodies
Katsumi Matsuzaki (1998)
Magainins as paradigm for the mode of action of pore forming polypeptides.Biochimica et biophysica acta, 1376 3
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.
Febs Letters – Wiley
Published: Nov 23, 2001
Keywords: ; ; ; ; ; ; ; ; ; ; ; ; ;
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