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PubMed2003

Lactoferrin against Staphylococcus aureus Mastitis. Lactoferrin alone or in combination with penicillin G on bovine polymorphonuclear function and mammary epithelial cells colonisation by Staphylococcus aureus.

Antibiotics should combine good antibacterial activity and the capacity to work in association with the host defence system. In this study, we have investigated the effects of bovine lactoferrin alone or in combination with penicillin G on the phagocytic activity of bovine polymorphonuclear leukocytes against Staphylococcus aureus. We have shown that susceptibility of S. aureus to phagocytosis was decreased in the presence of penicillin in the medium. In a kinetic study, lactoferrin alone did not affect phagocytosis but, when used with penicillin, it reversed the negative effect of this antibiotic on phagocytosis. In addition, in an epithelial invasion assay, lactoferrin alone or in combination with penicillin reduced the invasion of mammary epithelial cells in culture by S. aureus. Lactating female CD-1 mice were infected by intra-mammary delivery of a virulent penicillin-susceptible S. aureus strain and were then randomly assigned to treatments according to a 2 x 2 factorial design. In this mouse mastitis model, 2 days of systemic treatments with lactoferrin and/or penicillin did not lead to a total clearance of infection by S. aureus, but bacterial number was significantly reduced by treatments with lactoferrin or penicillin. These data suggest that bovine lactoferrin, alone or in combination with penicillin G, enhances S. aureus susceptibility to immuno-defense mechanisms, which can be beneficial in the treatment of S. aureus infections.

Animals↗

PubMed1985

Lactoferrin in plasma measured by an ELISA technique: evidence that plasma lactoferrin is an indicator of neutrophil turnover and bone marrow activity in acute leukaemia.

This study describes an ELISA technique with high specificity, sensitivity, accuracy and reproducibility for measurements of plasma lactoferrin. The detection limit was 0.001 microgram/ml and the median value obtained in EDTA plasma from 47 healthy adults was 0.100 microgram/ml (0.05 fractile: 0.046 microgram/ml, 0.95 fractile: 0.257 microgram/ml). The lactoferrin concentration in serum was on the average 2 1/2 times higher than in plasma. The ambient temperature did not influence the plasma concentration during the first 6 h from blood sampling to separation of plasma from the cells. In 8 patients with untreated acute leukaemia plasma lactoferrin was positively correlated to the peripheral neutrophil count. An almost parallel course in plasma lactoferrin and peripheral neutrophil number was observed in 4 patients with AML during chemotherapy. In 2 patients achieving complete remission, plasma lactoferrin increased about 6 d before the concomitant increase in neutrophil count, suggesting plasma lactoferrin as an early predictor of bone marrow regeneration.

Adolescent↗

PubMed1992

The N-linked oligosaccharides of human lactoferrin are not required for binding to bacterial lactoferrin receptors.

The oligosaccharides of human lactoferrin were enzymatically removed with glycopeptidase F, resulting in a preparation containing partial and fully deglycosylated human lactoferrin. The derivatives were separated by Concanavalin A affinity chromatography and compared with native human lactoferrin with respect to their ability to bind to bacterial receptors. Competitive binding experiments demonstrated that the lactoferrin derivatives were equally capable as native lactoferrin in binding to receptors of Neisseria meningitidis, Neisseria gonorrhoeae, and Moraxella catarrhalis. This result indicates that the oligosaccharides on human lactoferrin are not essential for binding to the bacterial receptors.

Binding Sites↗

PubMed1995

Isolation and characterization of sheep lactoferrin, an inhibitor of platelet aggregation and comparison with human lactoferrin.

Highly purified sheep lactoferrin was isolated from ovine whey in a single chromatographic step (FPLC): it was characterized by electrophoresis, N-terminal sequence determination and compared with lactoferrins from other species. Sheep and human lactoferrins inhibited thrombin-induced platelet aggregation (median inhibitory concentration: IC50 5 and 4 microM, respectively). Pepsin hydrolysates of human and sheep lactoferrins were fractionated by reverse-phase high-performance liquid chromatography and only one peak was an inhibitor of platelet aggregation. The sheep or human lactoferrin binding to platelets was studied.

Amino Acid Sequence↗

PubMed2001

Differential pattern in circulating nitrogen derivatives, lactoferrin, and anti-lactoferrin antibodies in HIV type 1 and HIV type 2 infections.

HIV-1 infection is associated with a dramatic reduction in antioxidative molecules both at the cellular level and in the circulation. This is particularly so for lactoferrin, an iron-binding protein involved in natural defenses (antimicrobial and antiviral activities, etc.) and found in whole secretions, including milk and mucus. In addition to its ability to chelate iron ions, lactoferrin inhibits hydroxy radical formation and interacts with nitric oxide (NO). Levels of plasma lactoferrin decreased in HIV-1-infected patients in correlation with progression of the disease, and highly specific anti-lactoferrin autoantibodies increased. This profile was specific to HIV-1 infection; it was not found in HIV-2-infected patients. In parallel with the drop in lactoferrin, a marked increase in circulating nitrogen derivatives was observed in HIV-1-infected patients, whereas low levels were found in normal donors and in HIV-2-infected patients. These data suggested hyperstimulation of the NO pathway throughout HIV-1 but not HIV-2 infection. This overproduction of NO could play an important role in the development of AIDS symptoms and signs.

Antibodies, Antineutrophil Cytoplasmic↗

PubMed1995

Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein.

Bacterial transferrin receptors that have been described in the families Pasteurellaceae and Neisseriaceae are composed of two receptor proteins, transferrin binding proteins 1 and 2 (Tbp1 and Tbp2). In contrast, bacterial lactoferrin receptors have only been described for human pathogens in the family Neisseriaceae, and were believed to consist of a single protein, Lbp1, which is highly homologous to Tbp1. We describe a modified affinity isolation procedure that facilities isolation of a second lactoferrin receptor protein Lbp2 (a presumptive Tbp2 homologue) from Neisseria meningitidis, Moraxella catarrhalis and Moraxella bovis using immobilized lactoferrin. Antiserum specific for either the M. catarrhalis Tbp1+2 molecules, the M. catarrhalis Lbp1 molecule, or for a commercial preparation of human lactoferrin did not react on western blots with the same organisms' affinity purified Lbp2. In addition, the M. catarrhalis Lbp2 could be isolated in a functional form without contaminating Lbp1 or Tbp1+2. We also demonstrate that the bovine pathogen, M. bovis, produces functional transferrin and lactoferrin receptors specific for the bovine forms of these glycoproteins. A putative lbpB gene, recently speculated to reside immediately upstream of the N. meningitidis Lbp1 structural gene, lbpA, likely encodes the newly isolated Lbp2 protein from this bacterial species.

Animals↗

PubMed1993

Regions located in both the N-lobe and C-lobe of human lactoferrin participate in the binding interaction with bacterial lactoferrin receptors.

As a first step in localizing the regions of human lactoferrin involved in binding to bacterial lactoferrin receptors, N-lobe and C-lobe fragments were assessed for binding to receptors on Neisseria meningitidis, Neisseria gonorrhoeae and Moraxella (Branhamella) catarrhalis. Preparations of N-lobe and C-lobe were obtained by tryptic digestion of iron-loaded human lactoferrin followed by separation of the two lobes by gel exclusion chromatography in 10% acetic acid. Solid phase binding studies demonstrated that the isolated C- and N-lobe preparations were capable of binding to membranes from iron-deficient N. meningitidis, N. gonorrhoeae and M. catarrhalis. The binding of the individual C- and N-lobes was confirmed by an analytical SDS-PAGE binding method in which the membrane-associated polypeptides were identified by prior biotinylation and subsequent binding of labelled streptavidin. This contrasts with bacterial transferrin receptors, which only bind to C-lobe fragment of human transferrin, indicating that the bacterial lactoferrin and transferrin receptors differ in their interaction with their respective glycoprotein ligands and may differ in the mechanism of iron removal.

Biotin↗

PubMed2003

Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe.

Pathogenic bacteria in the family Neisseriaceae express surface receptors to acquire iron from the mammalian iron-binding proteins. Transferrins and lactoferrins constitute a family of iron-binding proteins highly related in both sequence and structure, yet the bacterial receptors are able to distinguish between these proteins and uphold a strict binding specificity. In order to understand the molecular basis for this specificity, the interaction between human lactoferrin (hLf) and the lactoferrin-binding protein A (LbpA) from Moraxella catarrhalis was studied. A periplasmic expression system was designed for the heterologous expression of LbpA, which enabled the investigation of its binding activity in the absence of lactoferrin-binding protein B (LbpB). To facilitate delineation of the LbpA-binding regions of hLf, chimeric proteins composed of hLf and bovine transferrin were made. Binding studies performed with the chimeric proteins and recombinant LbpA identified two binding regions within the C-terminus of hLf. Furthermore, native LbpA from Moraxella and Neisseria spp. bound the identical spectrum of hybrid proteins as the recombinant receptor, demonstrating a conserved binding interaction with the C-lobe of hLf.

Amino Acid Sequence↗

PubMed2001

Interactions of bismuth with human lactoferrin and recognition of the Bi(III)-lactoferrin complex by intestinal cells.

Several bismuth compounds are currently used as antiulcer drugs, but the mechanism of action still remains unclear. The antimicrobial activity of Bi(III) complexes toward Gram-negative bacteria is reported to be dependent on the iron uptake system [Domenico, P., et al. (1996) J. Antimicrob. Chemother. 38, 1031-1040]. Electronic absorption and 13C NMR spectroscopic data show that Bi(III) binds to human lactoferrin at the specific Fe(III) sites along with either carbonate or oxalate as the synergistic anion. The uptake of Bi(III) by apo-hLF was rapid [minutes in 10 mM Hepes buffer and 5 mM bicarbonate (pH 7.4)], and almost equal in both lobes. The presence of ATP facilitates the release of Bi(III) from the Bi2-hLF complex when the pH is lowered. The Bi2-hLF complex blocked the uptake of the radiolabeled 59Fe-hLF complex into rat IEC-6 cells. Surprisingly, apo-hLF (but not apotransferrin) was almost as effective in blocking 59Fe uptake as bismuth-loaded lactoferrin. These results suggest that Bi(III)-loaded hLF might be recognized by the lactoferrin receptor and be taken up into cells.

Adenosine Triphosphate↗

PubMed1999

Lactoferrin-metal interactions: first crystal structure of a complex of lactoferrin with a lanthanide ion (Sm3+) at 3.4 A resolution.

Lactoferrin is an important member of the transferrin family. A characteristic property of transferrins is their ability to bind very tightly (K(app) approximately/= 10(20)) but reversibly two Fe(3+) ions. The structural consequences of binding a metal other than Fe(3+) have been examined by crystallographic analysis at 3.4 A resolution of mare samarium-lactoferrin (Sm(2)Lf). The structure was refined to an R factor of 0.219 for 8776 reflections in the resolution range 17.0-3.4 A. The samarium geometry (distorted octahedral coordination) is similar in both lobes. However, the anion interactions are quite different in the two lobes. In the N lobe, the anion is able to form only two hydrogen bonds instead of the four observed in the C lobe of Sm(2)Lf and the six observed in Fe(2)Lf. This is because Arg121, Thr117 and Gly124 have moved away from the anion as a consequence of the binding of the Sm(3+) ion. The protein ligands in the binding cleft of Sm(2)Lf show large displacements, but the overall protein structure remains the same. The binding of Sm(3+) by lactoferrin shows that the protein is capable of sequestering ions of different sizes and charges, though with reduced affinity. This conclusion should be true of other transferrins also.

Animals↗

PubMed1997

Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice.

We investigated the effect of a bovine milk protein, lactoferrin (LF-B), and a pepsin-generated peptide of LF-B, lactoferricin (Lfcin-B), on inhibition of tumor metastasis produced by highly metastatic murine tumor cells, B16-BL6 melanoma and L5178Y-ML25 lymphoma cells, using experimental and spontaneous metastasis models in syngeneic mice. The subcutaneous (s.c.) administration of bovine apo-lactoferrin (apo-LF-B, 1 mg/mouse) and Lfcin-B (0.5 mg/mouse) 1 day after tumor inoculation significantly inhibited liver and lung metastasis of L5178Y-ML25 cells. However, human apolactoferrin (apo-LF-H) and bovine holo-lactoferrin (holo-LF-B) at the dose of 1 mg/mouse failed to inhibit tumor metastasis of L5178Y-ML25 cells. Similarly, the s.c. administration of apo-LF-B as well as Lfcin-B, but not apo-LF-H and holo-LF-B, 1 day after tumor inoculation resulted in significant inhibition of lung metastasis of B16-BL6 cells in an experimental metastasis model. Furthermore, in in vivo analysis for tumor-induced angiogenesis, both apo-LF-B and Lfcin-B inhibited the number of tumor-induced blood vessels and suppressed tumor growth on day 8 after tumor inoculation. However, in a long-term analysis of tumor growth for up to 21 days after tumor inoculation, single administration of apo-LF-B significantly suppressed the growth of B16-BL6 cells throughout the examination period, whereas Lfcin-B showed inhibitory activity only during the early period (8 days). In spontaneous metastasis of B16-BL6 melanoma cells, multiple administration of both apo-LF-B and Lfcin-B into tumor-bearing mice significantly inhibited lung metastasis produced by B16-BL6 cells, though only apo-LF-B exhibited an inhibitory effect on tumor growth at the time of primary tumor amputation (on day 21) after tumor inoculation. These results suggest that apo-LF-B and Lfcin-B inhibit tumor metastasis through different mechanisms, and that the inhibitory activity of LF-B on tumor metastasis may be related to iron (Fe3+)-saturation.

Animals↗

PubMed1987

Diagnostic and prognostic significance of serum measurements of lactoferrin, lysozyme and myeloperoxidase in acute myeloid leukemia (AML): recognition of a new variant, high-lactoferrin AML.

92 patients with acute myeloid leukemia were classified according to the FAB classification (M1 n = 20, M2 n = 43, M3 n = 1, M4 n = 19, M5a n = 2, M5b n = 2, and M6 n = 5 patients). Serum measurements of lactoferrin (LF), myeloperoxidase (MPO) and lysozyme (LYS) were performed before the start of treatment. LF was significantly lower in M1 when compared with M2 but not as compared to M4, MPO was significantly higher in M2 and M4 than in M1, but comparable MPO levels were found in M2 and M4. LYS was significantly elevated in M2 in comparison with M1, and in M4 when compared to both M1 and M2. Polymorphonuclear granulocytes (PMNs) in M1 were significantly reduced when compared with M2 and M4, whereas mononuclear cells were significantly increased in M4 in comparison with both M1 and M2. FAB classification did not generate any prognostic information. When the patients were, instead, subdivided according to LF levels were found prognostically significant differences. Of patients below 100 micrograms/l, 44% went into remission as compared to 77% with LF from 101 to 400 micrograms/l. In patients with LF levels above 400 micrograms/l the remission frequency was only 14%. Multivariate statistical analysis on the data further suggested that lactoferrin may be used as an independent prognostic indicator. We conclude that although determination of the serum-levels of lactoferrin, lysozyme and myeloperoxidase in certain cases may be valuable as a supplement to the morphological examination of acute myeloid leukemia, it is evident that none of the three determinations can be used alone to distinguish between the FAB groups.

Adult↗

PubMed2006

Isolation of bovine lactoferrin, lactoperoxidase and enzymatically prepared lactoferricin from proteolytic digestion of bovine lactoferrin using adsorptive membrane chromatography.

A new downstream procedure for the isolation of bovine lactoferrin (bLf), lactoperoxidase and bovine lactoferricin (LfcinB) from sweet cheese whey was developed at the laboratory scale, based on membrane adsorber technology. The procedure was upscaled later on to an industrially relevant scale for the purificationof sweet whey concentrate with a recovery yield for lactoferrin of more than 90%. Based on these results the industrial process for 1 x 10(8) kg whey per year was projected. These high-value proteins were downstreamed by using cation-exchange membrane systems (Sartobind S, Sartorius, Göttingen, Germany). These strongly acidic membranes trap proteins in its anionic form. The dynamic loading capacity for both proteins as well as the optimal elution profiles with sodium chloride gradients were derived from laboratory experiments using membrane modules with 15-75 cm2 membrane material. Further investigations were performed with 1 m2 modules in a continuous process mode. The enzymatic preparation of LfcinB from bLf was performed by pepsin hydrolysis and the isolation of LfcinB was directly carried out from the enzymatic digest mixture. The identification of the proteins was performed with matrix-assisted laser desorption ionisation mass spectrometry (MALDI-MS). LfcinB and bLf were both tested afterwards in biological assays in order to show not only the efficiency of the downstreaming process in regard to product quantity but also to product quality (biological activity).

Adsorption↗

PubMed2002

"Dilysine trigger" in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin.

The mammalian iron-binding proteins lactoferrin (Lf) and transferrin (Tf) bind iron very tightly, but reversibly. Despite homologous structures and essentially identical iron binding sites, Tf begins to release iron at pH 6.0, whereas Lf retains iron to pH approximately 3.5. This difference in iron retention gives the two proteins different biological roles. Two lysine residues, Lys 206 and Lys 296, which form a hydrogen-bonded dilysine pair in human Tf, have been shown to strongly influence iron release from the N-lobe. The equivalent residues in human Lf are Arg 210 and Lys 301, and we have here mutated Arg 210 in the N-lobe half-molecule of human lactoferrin, Lf(N), to probe its role in iron release. The Lf(N) mutants R210G, R210E, and R210L were expressed, purified, and crystallized, and their crystal structures were determined and refined at resolutions of 1.95 A (R210G), 2.2 A (R210E), and 2.0 A (R210L). The overall structures are very similar to that of wild-type Lf(N), but with small differences in domain orientations. In each of the mutants, however, Lys 301 (equivalent to Lys 296 in Tf) changes its conformation to fill the space occupied by Arg 210 Neta2 in wild-type Lf(N), interacting with the two tyrosine ligands Tyr 92 and Tyr 192. By comparison with other Lf and Tf structures, we conclude that Lys 301 (or Lys 296 in Tf) only occupies this site when residue 210 (206 in Tf) is nonpositive (neutral as in R210G and R210L or negative as in R210E). Thus, Lys 206 in the Tf dilysine pair is identified as having a depressed pK(a). Three specific sites are variably occupied by polar groups in the Lf mutants and other Lf and Tf proteins, and when coupled with iron-release data, these give new insights into the factors that most influence iron retention at low pH.

Amino Acid Substitution↗

PubMed1999

High-level expression of human lactoferrin in milk of transgenic mice using genomic lactoferrin sequence.

In our previous study, transgenic mice were generated that expressed human lactoferrin (hLF) in milk using cDNA under control of the 2 kb bovine beta-casein promoter. The expression level of the protein in milk of 7 mice ranged from 1 to 200 microg/ml; 1 to 34 microg/ml in 6 mice and 200 microg/ml in 1 mouse. With the aim of inducing higher expression of the protein, we constructed an expression cassette comprised of 10 kb of the bovine beta-casein gene promoter and the hLF genomic sequence in place of the cDNA. The hLF genomic sequence of about 27 kb, spanning 23 kb of the entire coding region and 4 kb of the 3'-flanking sequence, was placed downstream the bovine beta-casein promoter. In total, 8 transgenic mice were generated from 31 mice (transgenic rate of 25.8%) born from the embryos microinjected with the 40-kb hLF expression cassette. Mammary-specific expression of the transgene was addressed by performing Northern hybridization of the total RNAs from various tissues of transgenic mice. Immunoblot analysis showed that the recombinant protein expressed in milk has the same molecular weight as the native protein. The amount of the protein in milk of 5 mice ranged from 60 to 6,600 microg/ml when judged by ELISA analysis. Three mice expressed the protein at the level higher than 500 microg/ml. These data suggest that the genomic lactoferrin sequence represents a valuable element for the efficient expression of the protein in milk of transgenic animals.

Animals↗

PubMed2003

Expression of bovine lactoferrin and lactoferrin N-lobe by recombinant baculovirus and its antimicrobial activity against Prototheca zopfii.

Lactoferrin (LF) is a multifunctional, iron-binding glycoprotein found in secretory fluids of mammals. In this study, DNA encoding bovine lactoferrin (bLF) or the N-terminal half of bLF (bLF N-lobe) was inserted into a baculovirus transfer vector, and a recombinant virus expressing bLF or bLF N-lobe was isolated. An 80-kDa bLF-related protein expressed by the recombinant baculovirus was detected by monoclonal antibodies against bLF N-lobe and the C-terminal half of bLF (bLF C-lobe). A 43-kDa bLF N-lobe-related protein expressed by the recombinant baculovirus was detected by anti-bLF N-lobe monoclonal antibody, but not by anti-bLF C-lobe monoclonal antibody. These proteins were also secreted into the supernatant of insect cell cultures. Recombinant bLF (rbLF) and bLF N-lobe (rbLF N-lobe) were affected by tunicamycin treatment, indicating that rbLF and rbLF N-lobe contain an N-linked glycosylation site. Antimicrobial activity of these recombinant proteins against Prototheca zopfii (a yeast-like fungus that causes bovine mastitis) was evaluated by measuring the optical density of the culture microplate. Prototheca zopfii was sensitive to rbLF and rbLF N-lobe, as well as native bLF. There was no difference in antimicrobial activity between rbLF N-lobe and bLF C-lobe.

Animals↗

PubMed1987

Lactoferrin effects of phagocytic cell function. II. The presence of iron is required for the lactoferrin molecule to stimulate intracellular killing by macrophages but not to enhance the uptake of particles and microorganisms.

Human lactoferrin (LF)--a neutrophil glycoprotein, the body fluid levels of which increase in inflammatory conditions--stimulates the phagocytic and cytotoxic properties of macrophages. We found in this work that, whereas the presence of iron in the LF molecule was not required to increase the capacity of mouse peritoneal macrophages (MPM) to take up Trypanosoma cruzi amastigotes (AMA), Listeria monocytogenes, or latex particles, it was necessary for LF to enhance intracellular killing of the two microorganisms. Thus, iron-free human lactoferrin (ApoLF), which did not increase MPM cytotoxicity, after restoration of ferric ions prior to its use in MPM treatments or when ferric citrate was added to the culture medium immediately after ApoLF treatment of the MPM, does increase MPM cytotoxicity. In that iron ions cannot be internalized as such, the latter observation suggested that ApoLF had taken up iron while membrane bound and then enhanced killing. Immunofluorescence studies revealed that comparable proportions of MPM-bound ApoLF or LF at either 20 or 100% iron saturation without appreciable differences in fluorescence intensity. Therefore, reduced binding of ApoLF compared with LF was not a likely explanation for the lack of effect of ApoLF on MPM killing. LF did not enhance AMA killing by MPM in the presence of the iron chelator deferoxamine. Diethylaminetriamine-pentaacetic acid, an iron chelator which is not incorporated into cells, had a similar effect. The iron-binding protein transferrin did not alter the capacity of MPM to either take up or kill the AMA, indicating that the noted LF effects were not shared by all iron-binding proteins. However, prior treatment of MPM with transferrin enabled the cells to display a greater parasite killing capacity after ApoLF treatment, suggesting a role for iron in this activity. Whether iron is required for LF to impart the signal that elicits enhanced killing, to satisfy a biochemical requirement for more effective killing, or both, remains to be clarified. We also found that killing of internalized AMA by LF-treated MPM--previously reported to be mediated in part by H2O2, O2-., and 1O2--was inhibitable by scavengers of OH., and therefore, appears to involve this oxygen metabolite as well.

Animals↗

PubMed2006

Human and bovine lactoferrins in the milk of recombinant human lactoferrin-transgenic dairy cows during lactation.

Seven Friesian human lactoferrin (hLf)-transgenic primiparous dairy cows expressing recombinant hLf (rhLf) in their milk were included in the study. After calving, concentrations of rhLf and bovine LF (bLf) in the milk, somatic cell count and milk yield were determined. The concentration of rhLf was found to be constant, about 2.9 mg/mL, throughout the early lactation period of 3 months. The concentration of bLf in colostrum was higher after calving, but decreased rapidly during the first days of lactation. The mean concentration of bLf was 0.15 mg/mL, but concentrations varied between cows from 0.07 mg/mL to 0.26 mg/mL. Based on that, it may be possible to improve the non-specific host defence mechanism in the mammary gland of dairy cows by enhancing the content of rhLf in the milk.

Animals↗