Lactoferrin—a multifunctional protein with antimicrobial properties

Farnaud, Sébastien; Evans, Robert W.

doi:10.1016/s0161-5890(03)00152-4

Cited by 630 publications

(504 citation statements)

References 75 publications

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“…These include proteins and peptides, such as lysozyme and defensins, which kill bacteria (17)(18)(19). Host defenses also include specific anti-biofilm defense molecules, including lactoferrin (20), which chelates iron and prevents the development of P. aeruginosa biofilms (21). Given the importance of quorum sensing for bacterial virulence, we wondered whether mammalian cells have also developed defense mechanisms that target this communication system.…”

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confidence: 99%

Inactivation of a Pseudomonas aeruginosa quorum-sensing signal by human airway epithelia

Chun

Ozer

Welsh

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

266

181

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Mammalian airways protect themselves from bacterial infection by using multiple defense mechanisms including antimicrobial peptides, mucociliary clearance, and phagocytic cells. We asked whether airways might also target a key bacterial cell-cell communication system, quorum-sensing. The opportunistic pathogen Pseudomonas aeruginosa uses two quorum-sensing molecules, N-(3-oxododecanoyl)-L-homoserine lactone (3OC12-HSL) and Nbutanoyl-L-homoserine lactone (C4-HSL), to control production of extracellular virulence factors and biofilm formation. We found that differentiated human airway epithelia inactivated 3OC12-HSL. Inactivation was selective for acyl-HSLs with certain acyl side chains, and C4-HSL was not inactivated. In addition, the capacity for inactivation varied widely in different cell types. 3OC12-HSL was inactivated by a cell-associated activity rather than a secreted factor. These data suggest that the ability of human airway epithelia to inactivate quorum-sensing signal molecules could play a role in the innate defense against bacterial infection.

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confidence: 99%

Inactivation of a Pseudomonas aeruginosa quorum-sensing signal by human airway epithelia

Chun

Ozer

Welsh

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

266

181

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“…Such multifunctional ability of immuneassociated genes is not unknown in crustaceans (Destoumieux-Garzon et al, 2001;Lee et al, 2003;Lee et al, 2004) and is widely observed in other species (Gallo et al, 1994;Bals and Wilson, 2003;Boman, 2003;Farnaud and Evans, 2003;Kamysz et al, 2003;Koczulla et al, 2003). A useful step towards investigating the possible biological roles of this WAP-containing protein in crustaceans, as well as investigating the role of the putative signal sequence, is to express the protein recombinantly.…”

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confidence: 99%

Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas

Brockton

Hammond

Smith

2007

Molecular Immunology

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Carcinin is a whey acidic protein (WAP) domain-containing antimicrobial protein, produced by the circulating haemocytes of the shore crab, Carcinus maenas. Cloning of its full coding cDNA reveals that it shows some similarity to invertebrate defensins and has a valine-rich signal sequence followed by a defined cleavage site but no obvious acidic anionic 'pro' sequence. The C-terminus exhibits a unique cysteine array that is predicted to form 6 disulphide bonds in the tertiary structure. This 12 cysteine array arrangement is conserved in ESTs from related genera and seems to represent a novel tertiary structure amongst AMPs, unique to the Crustacea. There are at least 5 putative isoforms of the mature protein that may arise through the transcription of one or two alleles of a multi-exon gene. Several of the same transcripts have been found in different animals. These isoforms do not arise as a result of alternate splicing of the exons, but by the transcription of different alleles and /or single point mutation of the transcript at up to four loci in the gene. The most commonly expressed transcript of the protein was recombinantly expressed in bacterial fusion system to a yield of ca 2-3 µg ml -1 of culture. In vitro expression with or without the leader sequence confirms the bioinformatic prediction that the stability of the mature protein is reduced when the leader sequence is removed. Carcinin is one of very few invertebrate AMPs characterised at the gene, transcript and protein level and to be recombinantly expressed in vitro in a bacterial system.

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“…Lactoferrin consists of a single polypeptide chain having a molecular mass of about 80 kDa and it possesses two iron ion-binding sites per molecule [1]. Bacteriostatic and bactericidal activities of lactoferrin against Gram positive and Gram negative bacteria, some yeasts, fungi [2,5,6], parasite [29] and virus [18] have been reported. Moreover, several physiological functions of lactoferrin including modulation of the inflammatory response, activation of the immune system and control of myelopoiesis have been reported as reviewed in many articles [4,23,30].…”

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confidence: 99%

“…Moreover, several physiological functions of lactoferrin including modulation of the inflammatory response, activation of the immune system and control of myelopoiesis have been reported as reviewed in many articles [4,23,30]. The mechanism of the antimicrobial activity of lactoferrin has been understood to involve its iron ion chelating properties, making this essential factor inaccessible to invading pathogens [6,7], and to involve their membrane binding properties, causing the release of lipopolysaccharides from Gram negative bacteria [5]. It is known that the lactoferrin content is high not only in colostrum [12,20,27] but in the milk of non-lactating period [12,26] and in mastitic milk [10,24,25].…”

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confidence: 99%

“…In some cases, bacteria can intake such peptides as nutrients for their growth but it cannot be denied the production of a strong antimicrobial peptide, lactoferricin [3]. Moreover, it is known that certain microorganisms have lactoferrin-binding proteins or lactoferrin-receptor on their surface [6,9]. And S. aureus is one of bacteria possessing lactoferrin-receptor [15,16].…”

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confidence: 99%

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Susceptibilities against Bovine Lactoferrin with Microorganisms Isolated from Mastitic Milk

Lee

Kawai²,

Nakamura

et al. 2004

The Journal of Veterinary Medical Science

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ABSTRACT. Antibacterial effects of bovine lactoferrin were studied in vitro against microorganisms isolated from mastitic milk in Tokachi area, Hokkaido, Japan. Microorganisms isolated were Eschelichia coli (11 isolates), Klebsiella pneumoniae (5 isolates), enterococci (8 isolates), Staphylococcus aureus (10 isolates), coagulase negative staphylococci (CNS, 13 isolates), streptococci (11 isolates), Prototheca zopfii (7 isolates) and yeast-like fungi (9 isolates). Lactoferrin has been known as a multifunctional protein and its antimicrobial effect is one of the most essential function of it. In order to compare their susceptibilities against lactoferrin, the minimal inhibitory concentration values were estimated by a microplate assay method using 96-well microplate, which involved measuring the optical density of the cultures. Prototheca zopfii was highly sensitive to bovine lactoferrin and complete inhibition of this microorganism was observed even at the low concentration of 7 µg/ml. On the other hand, E. coli and enterococci showed resistance against lactoferrin action and staphylococci showed strain-dependent resistance. KEY WORDS: antimicrobial activity, lactoferrin, mastitic milk.

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Lactoferrin—a multifunctional protein with antimicrobial properties

Cited by 630 publications

References 75 publications

Inactivation of a Pseudomonas aeruginosa quorum-sensing signal by human airway epithelia

Inactivation of a Pseudomonas aeruginosa quorum-sensing signal by human airway epithelia

Gene characterisation, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas

Susceptibilities against Bovine Lactoferrin with Microorganisms Isolated from Mastitic Milk

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