Ultrastructural effects of antimicrobial peptides from bovine lactoferrin on the membranes of Candida albicans and Escherichia coli

Antimicrobial peptides allegedly exert their action on microbial membranes. Bovine lactoferrin enfold two antimicrobial domains, lactoferricin B (LFcin B) and lactoferrampin (LFampin). Effects of representative peptides thereof on the membranes of Candida albicans and Escherichia coli were investiga...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2005-09, Vol.26 (9), p.1537-1542
Main Authors: van der Kraan, Marieke I.A., van Marle, Jan, Nazmi, Kamran, Groenink, Jasper, van ’t Hof, Wim, Veerman, Enno C.I., Bolscher, Jan G.M., Amerongen, Arie V. Nieuw
Format: Article
Language:English
Subjects:
Animals
Antimicrobial Cationic Peptides - pharmacology
Biological and medical sciences
Candida albicans
Candida albicans - cytology
Candida albicans - drug effects
Candida albicans - ultrastructure
Cattle
Cell Division - drug effects
Cell Membrane - drug effects
Cell Membrane - ultrastructure
Confocal microscopy
Escherichia coli
Escherichia coli - cytology
Escherichia coli - drug effects
Escherichia coli - ultrastructure
Fluorescein-5-isothiocyanate - chemistry
Freeze Fracturing
Freeze-fracture electron microscopy
Fundamental and applied biological sciences. Psychology
Lactoferrampin
Lactoferricin
Lactoferrin
Lactoferrin - chemistry
Lactoglobulins - chemistry
Microscopy, Confocal
Microscopy, Electron - methods
Peptide Fragments - chemistry
Peptide Fragments - pharmacology
Vertebrates: endocrinology
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Summary:Antimicrobial peptides allegedly exert their action on microbial membranes. Bovine lactoferrin enfold two antimicrobial domains, lactoferricin B (LFcin B) and lactoferrampin (LFampin). Effects of representative peptides thereof on the membranes of Candida albicans and Escherichia coli were investigated. Confocal laser scanning microscopy revealed that these peptides were internalized within a few minutes, concurrently with disrupting membrane integrity as indicated by freeze-fracture transmission electron microscopy. The most striking findings were induction of distinct vesicle-like structures in the membrane of C. albicans by the LFampin peptide, and detachment of the outer membrane and surface protrusions in E. coli by the LFcin B peptide.
ISSN:0196-9781
1873-5169
DOI:10.1016/j.peptides.2005.02.011