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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.

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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.

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

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.

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.

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.

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.

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.
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