-inflammatory impact without known adverse impacts. Lactoferrin is an endogenous glycoprotein found in mammals, and a member of the larger transferrin family which is found widely in both animals and birds [ 17 ]. Although the highest concentrations of lactoferrin are
In this study, we examined the relationship between levels of lactoferrin (LF) and IL-17 in human serum and breast milk and the development of allergy in children. LF and IL-17 levels were determined by ELISA in healthy (n=19) and allergic mothers (n=21) on the 5th day after delivery. Two years later, information on breastfeeding and allergic outcomes was collected by questionnaires from parents of both groups and district child care nurses. Significantly higher concentrations of LF were found in the breast milk of allergic mothers compared to the healthy controls. At 2 years of age, only those three infants became allergic from the atopic group in whose starting breast milk samples a very high LF level (306 μg mg–1 protein) or simultaneously elevated concentrations of LF and IL-17 were measured. These findings indicate that the very early measurement of LF and IL-17 levels in the breast milk of allergic mothers may help to predict the allergy development in their infants.
Lactoferrin (formerly known as lactotransferrin) (LF) is a non-heme iron-binding protein that is a part of the transferrin protein family, thus belonging to those protein capable of binding and transferring Fe 3
In this study, Lactobacillus pentosus expressing porcine lactoferrin (pLF) was tested for in vitro antibacterial activity and for its ability to enhance immunity induced by an orally administered Aujeszky’s disease virus (ADV) vaccine. The cDNA encoding N-terminus of pLF was cloned into a Lactobacillus-specific plasmid to produce L. pentosus pLF expressing transformants (pPG612.1-pLFN/ L. pentosus). The antimicrobial activity of the recombinant pLF protein inhibited bacterial growth in vitro. The supernatant of pPG612.1-pLF-N/L. pentosus had an inhibitory effect on Staphylococcus aureus strain CVCC26003, Bacillus subtilis strain CVCC63501, Escherichia coli strain CVCC10141 and Salmonella enterica ssp. entericaCholeraesuis strain CVCC79102, while it did not inhibit the growth of Lactobacillus casei strain ATCC393. A mouse model was established to test the effectiveness of the orally administered probiotic L. pentosus recombinant strain in the gastrointestinal tract. Mice were immunised with an attenuated porcine Aujeszky’s disease virus (ADV) vaccine. Serum antibody levels determined using a mouse Aujeszky’s disease IgG ELISA showed that IgG levels were significantly higher in the pPG612.1-pLFN/L. pentosus group than in the PBS and Lactobacillus pentosus groups at days 7 and 21 (P < 0.01) and at day 14 (P < 0.05), indicating that this oral recombinant strain can improve the effectiveness of the vaccine and play a role in immune enhancement through humoral immunity. These results suggest that the recombinant Lactobacillus pentosus not only has the beneficial characteristics of lactic acid bacteria but also produces biologically functional lactoferrin.
In this study susceptibility to different antimicrobial peptides was investigated on colistin-susceptible and colistin-resistant identical pulsotype strains of KPC-2 producing Klebsiella pneumoniae ST258 as well as colistin-susceptible and colistin-resistant Enterobacter asburiae strains isolated from clinical samples. In our test, bacteria were exposed to 50 mg/ml lactoferrin, lysozyme and protamine — cationic antimicrobial peptides belonging to innate immune system and having structural similarity to polymyxins — in separate reactions. After 18 hours incubation of colonies were counted. 40% of colistin-resistant K. pneumoniae strains and 97% of colistin-susceptible counterpart strains were lysed by protamine whereas 87% and 100% colony forming unit decrease by lysozyme was seen, respectively. In the case of colistin-resistant E. asburiae strains 1 log10 cell count increase were observed after treatment with lysozyme and 1.56 log10 after lactoferrin exposure compared to the initial number whereas the colistin-susceptible showed no relevant cell count increase. Our findings suggest that acquired colistin-resistance in Enterobacteriaceae is associated with tolerance against antimicrobial peptides.
Coagulation and inflammation are closely related as part of the mechanisms of host defence during a severe infection. The aim of this study was to investigate the relation between thrombin as a factor in both the coagulative and inflammatory processes and neutrophil secretory function on the basis of lactoferrin (LF), elastase and myeloperoxidase release in the course of mastitis and metritis in cows. Thrombin generation was measured on the basis of hydrolysis of SAR-PRO-ARG-pNA and lactoferrin concentration was estimated by an ELISA method. The greatest thrombin generation was observed in the metritis group (1.18 ± 0.62 IU). The level of LF was the highest in the group of cows with mastitis (0.74 ± 0.55 mg/ml) in the first phase of the disease. In the second phase of the diseases the level of serum LF in cows with mastitis diminished to the value of 0.41 ± 0.16 mg/ml, whereas in cows with metritis the level of LF increased to 0.51 ± 0.17 mg/ml. This study reveals that the excessive production of thrombin not only causes hypercoagulatory disorders but also exaggerates neutrophil function by the release of some enzymes which may play a destructive role during disseminated intravascular coagulation (DIC). These enzymes also inhibit anticoagulative systems, thus potentially worsening the course of the disease.
to each other ( El-Hatmi et al., 2023 ). Camel colostrum contains higher concentrations of whey proteins, particularly immunoglobulins G and lactoferrin, than camel milk. The lack of β-lactoglobulin, a whey protein in cow milk associated with