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
Clearance of Escherichia coli O157:H7 infection in calves by rectal administration of bovine lactoferrin
TL;DR: The results indicate that the use of bovine lactoferrin as a rectal treatment can be a useful strategy to preclude further transmission of EHEC infections from cattle to humans.
Patent
Lactoferrin variants and uses thereof
Orla M. Conneely,Pauline P. Ward +1 more
TL;DR: In this paper, the authors present an efficient and economical means for the production of recombinant lactoferrin variants and portions thereof, having modified iron-binding capacity, and to vectors comprising same recombinanat nucleic acids.
Journal ArticleDOI
Stochastic-based descriptors studying biopolymers biological properties: extended MARCH-INSIDE methodology describing antibacterial activity of lactoferricin derivatives.
Ronal Ramos de Armas,Humberto González Díaz,Humberto González Díaz,Reinaldo Molina,Reinaldo Molina,Eugenio Uriarte +5 more
TL;DR: The MARCH‐INSIDE methodology extended to peptide and proteins is applied to a QSAR study related to antibacterial activity of 31 derivatives of lactoffericin against E. Coli and S. Aureus by means of Linear Discriminant (LDA) and Multiple Linear Regression Analysis (MLR).
Journal ArticleDOI
C- and N-truncated antimicrobial peptides from LFampin 265 - 284: Biophysical versus microbiology results
TL;DR: Lactoferrin 265- 284 was the most active peptide toward the tested microorganisms, and in the biophysical studies it showed the highest ability to form an α-helix and the strongest interaction with model membranes, followed by LFampin 265 – 280.
Book ChapterDOI
The microbiological safety of raw milk
TL;DR: This chapter reviews the safety and benefits of raw milk and suggests that raw milk contains agents that inactivate pathogens, but many of these agents survive pasteurization and are present in pasteurized milk.
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.