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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Effects of lactoferricin B and cecropin P1 on growth performance, faecal score and dry matter in weaned piglets orally challenged with enterotoxigenic Escherichia coli F4
Zhen-Ping Hou,Wen-Jie Wang,Jing-xi Liu,Gang Liu,Zhi-qiang Liu,Wolfgang B. Souffrant,Vladimir Urubschurov,Jun Fan +7 more
TL;DR: Though there are no obvious effects, Lfcin B and Cec P1 have potential use without toxicity in vivo as additive in the husbandry product.
Human papillomavirus tropism
TL;DR: The aim of this thesis is to provide aonomy and classification of viral proteins and their role in the life cycle, as well as a history of the viral genome and its role in disease.
Dissertation
Development and evaluation of a beta-glucan biopolymer formulation of lactoferrin produced using a novel cryomilling technique
TL;DR: Any use you make of these documents or images must be for research or private study purposes only, and you may not make them available to any other person.
Journal ArticleDOI
Effect of in vitro gastrointestinal digestion on the antibacterial activity of bioactive dairy formulas supplemented with lactoferrin against Cronobacter sakazakii
TL;DR: In this paper , the effect of technological treatments and gastrointestinal digestion on the antibacterial activity against C. sakazakii of proteins present in dairy formulas supplemented with lactoferrin was analyzed.
CLINICAL ADVANCES IN LIVER, PANCREAS, AND BILIARY TRACT Ascitic Fluid Lactoferrin for Diagnosis of Spontaneous Bacterial Peritonitis
Mansour A. Parsi,Sherif Saadeh,Nizar N. Zein,Gary L. Davis,Rocio Lopez,James H. Boone,Maria R. Lepe,Linsheng Guo,Mohammad Ashfaq,Goran B. Klintmalm,Arthur J. McCullough +10 more
TL;DR: Qualitative bedside assays for the measurement of AFLAC can be developed easily and may serve as a rapid and reliable screening tool for SBP in patients with cirrhosis and a cut-off level that can be used for future development of a rapid bedside test.
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.