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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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Journal ArticleDOI

Effect of Cu/Mn-Fortification on In Vitro Activities of the Peptic Hydrolysate of Bovine Lactoferrin against Human Gastric Cancer BGC-823 Cells

TL;DR: Cu- and especially Mn-fortification of BLH brought health benefits such as increased anti-cancer activity in the BGC-823 cells via activating the apoptosis-related proteins to induce cell apoptosis.
Journal ArticleDOI

Histochemical properties of sialic acids and antimicrobial substances in canine anal glands

TL;DR: The localization of sialic acids and antimicrobial substances in the anal glands of dog was studied by sialoglycoconjugate histochemistry and immunohistochemistry to determine whether secretory products may create a defensive barrier against microbial invasion at the anal mucosa.
DissertationDOI

Effects of maternal subclinical mammary inflammation on infant growth

TL;DR: Three studies were carried out in Ghana with the overall aim of describing the mechanistic pathway(s) linking SCM and infant growth faltering, and whether SCM occurring beyond the third month postpartum had an adverse effect on infant growth between the third and sixth month post partum.

Antibacterial factors in cows’ milk and colostrum : immunoglobulins and lactoferrin

TL;DR: The pepsin digest of lactoferrin was bactericidal against Salmonella enteritidis in 1% peptone, but no substantial antibacterial activity could be demonstrated in trypticase soy broth or in some selected foods, raising doubts about the potential for addition of lactoferricin to foods.
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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