Effect of bovine lactoferrin on Chlamydia trachomatis infection and inflammation (original) (raw)
Related papers
Lactobacilli-Lactoferrin interplay in Chlamydia trachomatis infection
Pathogens and disease, 2017
In the cervico-vaginal micro-environment, lactobacilli are known to protect against genital infections and, amongst the host defence compounds, lactoferrin has recently acquired importance for its anti-microbial and anti-inflammatory properties. An abnormal genital micro-environment facilitates the acquisition of pathogens like Chlamydia trachomatis, the leading cause of bacterial sexually transmitted infections worldwide. The aim of our study is to investigate the effects of Lactobacillus crispatus, Lactobacillus brevis and bovine lactoferrin on chlamydial infection, in order to shed light on the complex interplay between host defence mechanisms and C. trachomatis. We have also evaluated the effect of these defence factors to modulate the chlamydia-mediated inflammatory state. To this purpose, we have determined the infectivity and progeny production of C. trachomatis as well as interleukin-8 and interleukin-6 synthesis. The main result of our study is that the combination of L. br...
Lactoferrin: Structure, function and applications
International journal of antimicrobial agents
Lactoferrin (LF) is an 80 kDa iron-binding glycoprotein of the transferrin family that is expressed in most biological fluids and is a major component of the mammalian innate immune system. Its protective effects range from direct antimicrobial activities against a large panel of microorganisms, including bacteria, viruses, fungi and parasites, to anti-inflammatory and anticancer activities. These extensive activities are made possible by mechanisms of action utilising not only the capacity of LF to bind iron but also interactions of LF with molecular and cellular components of both host and pathogens. This review summarises the putative antimicrobial mechanisms, clinical applications and heterologous expression models for LF.
Lactoferrin a multiple bioactive protein: An overview
Biochimica Et Biophysica Acta, 2011
Background: Lactoferrin (Lf) is an 80 kDa iron-binding glycoprotein of the transferrin family. It is abundant in milk and in most biological fluids and is a cell-secreted molecule that bridges innate and adaptive immune function in mammals. Its protective effects range from anticancer, anti-inflammatory and immune modulator activities to antimicrobial activities against a large number of microorganisms. This wide range of activities is made possible by mechanisms of action involving not only the capacity of Lf to bind iron but also interactions of Lf with molecular and cellular components of both hosts and pathogens. Scope of review: This review summarizes the activities of Lf, its regulation and potential applications. Major conclusions: The extensive uses of Lf in the treatment of various infectious diseases in animals and humans has been the driving force in Lf research however, a lot of work is required to obtain a better understanding of its activity. General significance: The large potential applications of Lf have led scientists to develop this nutraceutical protein for use in feed, food and pharmaceutical applications. This article is part of a Special Issue entitled Molecular Mechanisms of Iron Transport and Disorders.
Molecules, 2020
Due to the emergence of multidrug-resistant pathogens, it is necessary to develop options to fight infections caused by these agents. Lactoferrin (Lf) is a cationic nonheme multifunctional glycoprotein of the innate immune system of mammals that provides numerous benefits. Lf is bacteriostatic and/or bactericidal, can stimulate cell proliferation and differentiation, facilitate iron absorption, improve neural development and cognition, promote bone growth, prevent cancer and exert anti-inflammatory and immunoregulatory effects. Lactoferrin is present in colostrum and milk and is also produced by the secondary granules of polymorphonuclear leukocytes, which store this glycoprotein and release it at sites of infection. Lf is also present in many fluids and exocrine secretions, on the surfaces of the digestive, respiratory and reproductive systems that are commonly exposed to pathogens. Apo-Lf (an iron-free molecule) can be microbiostatic due to its ability to capture ferric iron, bloc...
A multifunctional bioactive protein: Lactoferrin
Lactoferrin which is also known by the name of lactotransferrin (LTF), is a multifunctional iron-binding glycoprotein of the transferrin family and is found in almost all human mucosal secretions as well as in the specific granules of polymorphonuclear leukocytes in blood. A variety of functions have been found to associated with this protein along with its contribution to antimicrobial host defense mechanism. Moreover, it has been shown to have direct effects on some of the pathogenic microorganisms through bacteriostatic and microbial iron uptake induction. Several studies have shown that the protein synergistically interacts with immunoglobins, complement, and neutrophil cationic proteins which act against Gram-negative bacteria. Further, both the whole protein and a cationic N-terminus peptide fragment directly damage the outer membrane of Gram-negative bacteria suggesting a mechanism for its supplemental antimicrobial effects. It has appeared logical that antimicrobial activity of the protein arises from sequestration of environmental iron thereby causing nutritional deprivation of iron in susceptible organisms. Lactoferrin has diverse role where it can be used as an immunotherapeutic and can also play a role in immunodiagnostics. Still its overall physiologic role remains yet to be defined clearly inside the living system.
Bovine lactoferrin and its functions in animals -A review
Agricultural Reviews, 2015
Lactoferrin (Lf) was discovered in 1939 as “red protein from milk whey”. Bovine lactoferrin (bLf) gene is located on Bos taurus autosome, long arm of chromosome no.22 (BTA 22q24) in cattle. Its size varies from 23-35kbp among different species. The lactoferrin gene consists of 17 exons and 16 introns ranging from 82bp (exon-1) to 225bp (exon-17). The presence of multiple regulatory elements within lactoferrin promoter contributes differential gene expression and variable content of lactoferrin in milk. The concentration of lactoferrin in normal bovine milk is about 0.02-0.2 mg/ml. The primary function of Lf lies in its role in iron metabolism including iron transport, storage and chelation. Lf exhibits strong antimicrobial activity against a broad spectrum of bacteria (gram-positive & negative), fungi, yeasts, viruses and parasites. Lf exerts bacteriostatic and bactericidal activity. Its main contribution to antiviral defence consists in its binding to the cell membrane glycosaminog...
MECHANISMS OF THE ANTIBACTERIAL ACTIVITY OF LACTOFERRIN AND LACTOFERRIN-DERIVED PEPTIDES
Lactoferrin (Lf), a member of the transferrin family of iron-binding proteins, is now known to have a number of properties, including antibacterial activity towards a broad spectrum of Gram-negative and Gram-positive bacteria. The mechanism of the antibacterial activity of Lf is complex and involves beside iron-chelation, direct action on bacteria and/or the activation of the immune system. Lactoferricin (Lfcin) and other peptides derived from Lf or Lfcin are more potent antibacterial agents, a property exhibited by interaction with and penetration of bacterial membrane. This article summarizes the current data on the mechanisms through which Lf and Lf-derived peptides exhibit their antibacterial activity.
Lactoferrin—a multifunctional protein with antimicrobial properties
Molecular Immunology, 2003
Lactoferrin is a member of the transferrin family of iron-binding proteins. Numerous functions have been reported and continue to be reported for the protein, some of which are related to its iron-binding properties. Its extensive antimicrobial activities were originally attributed to its ability to sequester essential iron, however, it is now established that it possesses bactericidal activities as a result of a direct interaction between the protein or lactoferrin-derived peptides. This article reviews the antimicrobial activities of lactoferrin and discusses the potential mode of action of lactoferrin-derived cationic peptides against Gram-negative bacteria in the light of recent studies.
Lactoferrin: potential functions, pharmacological insights, and therapeutic promises
Journal of Advanced Biotechnology and Experimental Therapeutics, 2021
ABSTRACT: Lactoferrin (LF) is an iron-binding multifunctional glycoprotein, act as a natural protective agent. In general, LF is involved in various physiological activities, including antibacterial, antifungal, antiviral, antiparasitic, anticarcinogenic and iron metabolism. The LF is most frequently found in milk as well as many other exocrine secretions such as saliva, bronchial mucus, seminal fluids, and gastrointestinal fluids, respectively. Increased expression and secretion of LF may play a significant role in the first line of host defense. One of the primary functions of LF is to scavenge free iron in fluids and inflamed areas to avoid free radical-facilitated damage. LF influences the proliferation, maturation, and activity of immune cells at the cellular level. LF plays a significant protective role in inflammation, oxidative stress, fibrosis, endoplasmic reticulum (ER) stress, autophagy dysfunction, and mitochondrial dysfunction. Also, LF was found protective against various pathologies including anemia, sepsis, and diarrhoea in clinical settings. This article reviews the protective role of LF against different pathophysiological conditions and its therapeutic advances as well as further research prospects.