Journal ArticleDOI
Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
TLDR
Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested, and Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.Abstract:
A physiologically diverse range of Gram-positive and Gram-negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 micrograms/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na+, K+, Mg2+ or Ca2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.read more
Citations
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Journal ArticleDOI
Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines.
TL;DR: It is shown that in vitro treatment with LfcinB rapidly induced apoptosis in several different human leukemia and carcinoma cell lines as determined by DNA fragmentation assays and phosphatidylserine headgroup inversion detected by Annexin V binding to the surface of cancer cells.
Journal ArticleDOI
Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule.
TL;DR: The results suggest a possible antimicrobial function of α-lactalbumin after its partial digestion by endopeptidases, and replacement of leucine with isoleucine in the sequence GYGGVSLPEWV CTTF ALC SEK significantly reduced the bactericidal capacity of the polypeptide.
Journal ArticleDOI
Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin.
Marieke I.A. van der Kraan,J. Groenink,Kamran Nazmi,Enno C. I. Veerman,Jan G. M. Bolscher,Arie V. Nieuw Amerongen +5 more
TL;DR: Lactoferrampin was active against Bacillus subtilis, Escherichia coli, and Pseudomonas aeruginosa, but not against the fermenting bacteria Actinomyces naeslundii, Porphyromonas gingivalis, Streptococcus mutans and Streptitis sanguis.
Journal ArticleDOI
Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
Wayne Robert Bellamy,Hiroyuki Wakabayashi,Mitsunori Takase,Kouzou Kawase,Seiichi Shimamura,Mamoru Tomita +5 more
TL;DR: Findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans and suggest the lethal effect of lactoferricin B results from its direct interaction with the cell surface.
Journal ArticleDOI
Lactoferrin: A Natural Glycoprotein Involved in Iron and Inflammatory Homeostasis
TL;DR: Human lactoferrin, an iron-binding multifunctional cationic glycoprotein secreted by exocrine glands and by neutrophils, inhibits intracellular iron overload, an unsafe condition enhancing in vivo susceptibility to infections, as well as anemia of inflammation (AI), re-establishing IIH.
References
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Journal ArticleDOI
Identification of the bactericidal domain of lactoferrin.
Wayne Robert Bellamy,Mitsunori Takase,Koji Yamauchi,Hiroyuki Wakabayashi,Kouzou Kawase,Mamoru Tomita +5 more
TL;DR: The studies suggest this domain is the structural region responsible for the bacterial properties of lactoferrin, having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 microM and 3.0 microM, depending on the target strain.
Journal ArticleDOI
All-D amino acid-containing channel-forming antibiotic peptides.
David Wade,Anita Boman,Birgitta Wahlin,Charles Michael Drain,David Andreu,Hans G. Boman,R. B. Merrifield +6 more
TL;DR: The D enantiomers of three naturally occurring antibiotics--cecropin A, magainin 2 amide, and melittin--were synthesized and it is suggested that the mode of action of these peptides on the membranes of bacteria, erythrocytes, plasmodia, and artificial lipid bilayers may be similar and involves the formation of ion-channel pores spanning the membranes, but without specific interaction with chiral receptors or enzymes.
Journal ArticleDOI
Cell-free immunity in insects.
Hans G. Boman,Dan Hultmark +1 more
TL;DR: The authors showed that at least two of the cecropins originate from a gene duplication and that the biosynthesis has been initiated on RNA and tissue levels on both RNA and DNA levels.
Journal ArticleDOI
Killing of gram-negative bacteria by lactoferrin and lysozyme.
rd R T Ellison,T. J. Giehl +1 more
TL;DR: Dialysis chamber studies indicate that bacterial killing requires direct contact with lactoferrin, and work with purified LPS suggests that this relates to direct LPS-binding by the protein, suggesting that their interaction contributes to host defense.
Journal ArticleDOI
A bactericidal effect for human lactoferrin
TL;DR: Streptococcus mutans and Vibrio cholerae, but not Escherichia coli, were killed by incubation with purified human apolact oferrin, contingent upon the metal-chelating properties of the lactoferrin molecule.