Free secretory component and lactoferrin of human milk inhibit the adhesion of enterotoxigenic Escherichia coli

Giugliano, Loreny Gimenes; Ribeiro, Sidarta; Vainstein, Marilene Henning; Ulhôa, Cirano José

doi:10.1099/00222615-42-1-3

Cited by 109 publications

(83 citation statements)

References 43 publications

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“…Adhesion of the strain possessing CFA I fimbriae, was inhibited by both, whole milk and NIgF, but not by the IgF, indicating the importance of NIgF on the adhesion of CFA I strains. These findings are corroborated by our previous studies (15,25), showing that lactoferrin and fSC present in the NIgF inhibit bacterial adhesion to erythrocytes, binding to bacterial fimbriae.…”

Section: Discussionsupporting

confidence: 81%

“…It has been shown that fSC is an 80 kDa glycoprotein, consisting of a single polypeptide chain largely glycosilated (20%) (19). There is little information about the role of fSC in secretions, but some workers suggest that it may have a protective role against diarrhea (4,15). Recently, using immunogold labeling, we showed the ability of fSC to interact with CFA I and CFA II (CS1 and CS3) fimbrial adhesins (25).…”

Section: Introductionmentioning

confidence: 99%

“…We demonstrated that human milk glycoproteins, such as lactoferrin and free secretory component (fSC), have the ability to inhibit adhesion of ETEC CFA I + strains to human erytrocytes (15).…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of enterotoxigenic Escherichia coli (ETEC) adhesion to Caco-2 cells by human milk and its immunoglobulin and non-immunoglobulin fractions

Oliveira¹,

Bessler²,

Báo³

et al. 2007

Braz. J. Microbiol.

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Enterotoxigenic Escherichia coli (ETEC) is the most common cause of diarrhea in children in developing countries and among travelers to ETEC endemic areas. ETEC diarrhea is caused by colonization of the small intestine mediated by colonization factor (CF) antigens, and subsequent elaboration of enterotoxins. Breast feeding has been related to protection against enteric infections. The protective effect of human milk can be ascribed to its immunoglobulin content, specially secretory immunoglobulin A (sIgA), and to nonimmunoglobulin components such as free oligosaccharides, glycoproteins and glycolipids. In this study we investigated the effect of whole human milk and its fractions immunoglobulin and non-immunoglobulin on the adherence of ETEC strains possessing different CFs to Caco-2 cells, as well as the ability of sIgA and free secretory component (fSC) to bind to bacterial superficial proteins. Pooled human milk from three donors were fractionated by gel filtration and analyzed by SDS-PAGE. Our results revealed that whole human milk and its proteins fractions, containing sIgA and fSC, inhibited adhesion ETEC strains harboring different colonization factors antigens. We also verified that sIgA and fSC, using immunoblotting and immunogold labeling assays, bound to some fimbrial proteins and other material present in bacterial surface. Our findings suggest that whole human milk and its fractions may contribute to protection against ETEC infections by blocking bacterial adhesion mediated by different colonization antigens.

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Section: Discussionsupporting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

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Inhibition of enterotoxigenic Escherichia coli (ETEC) adhesion to Caco-2 cells by human milk and its immunoglobulin and non-immunoglobulin fractions

Oliveira¹,

Bessler²,

Báo³

et al. 2007

Braz. J. Microbiol.

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“…In vivo studies have demonstrated the protective effects of fucosylated oligosaccharide fractions of human milk against heat stable enterotoxin of Escherichia coli in suckling mice (10). Clostridium difficile binds to glycosylated SC to a much greater extent than to the deglycosylated form (11), and the SC-dependent inhibition of adhesion of enterotoxic forms of E. coli to erythrocytes is apparently reliant on the carbohydrate portion of SC (12). Furthermore, removal of N-linked oligosaccharides from sIgA has been shown to enhance the fixation of C3b and activation of the alternative complement pathway (3).…”

Section: S Ecretory Component (Sc)mentioning

confidence: 99%

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

Marshall

Perks

Ferkol

et al. 2001

The Journal of Immunology

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The bronchial epithelium is a source of both α and β chemokines and, uniquely, of secretory component (SC), the extracellular ligand-binding domain of the polymeric IgA receptor. Ig superfamily relatives of SC, such as IgG and α2-macroglobulin, bind IL-8. Therefore, we tested the hypothesis that SC binds IL-8, modifying its activity as a neutrophil chemoattractant. Primary bronchial epithelial cells were cultured under conditions to optimize SC synthesis. The chemokines IL-8, epithelial neutrophil-activating peptide-78, growth-related oncogene α, and RANTES were released constitutively by epithelial cells from both normal and asthmatic donors and detected in high m.w. complexes with SC. There were no qualitative differences in the production of SC-chemokine complexes by epithelial cells from normal or asthmatic donors, and in all cases this was the only form of chemokine detected. SC contains 15% N-linked carbohydrate, and complete deglycosylation with peptide N-glycosidase F abolished IL-8 binding. In micro-Boyden chamber assays, no IL-8-dependent neutrophil chemotactic responses to epithelial culture supernatants could be demonstrated. SC dose-dependently (IC50 ∼0.3 nM) inhibited the neutrophil chemotactic response to rIL-8 (10 nM) in micro-Boyden chamber assays and also inhibited IL-8-mediated neutrophil transendothelial migration. SC inhibited the binding of IL-8 to nonspecific binding sites on polycarbonate filters and endothelial cell monolayers, and therefore the formation of haptotactic gradients, without effects on IL-8 binding to specific receptors on neutrophils. The data indicate that in the airways IL-8 may be solubilized and inactivated by binding to SC.

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“…Binding to E. coli colonization factors [36] causes inhibition of hemagglutination [37] and inhibition of adherence of ETEC to epithelial cells in vitro and to intestinal mucosa of germfree mice in vivo [38].…”

Section: Enterotoxigenic Escherichia Coli (Etec)mentioning

confidence: 99%

Effect of lactoferrin on enteric pathogens

Ochoa

Cleary²

2009

Biochimie

119

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Much has been learned in recent years about the mechanisms by which breastfeeding improves child health and survival. However, there has been little progress in using these insights to improve pediatric care. Factors that are important for protecting the breast fed infant might be expected to decrease the adverse effects of weaning on diarrhea, growth, and development. Lactoferrin, an ironbinding protein with multiple physiological functions (anti-microbial, anti-inflammatory, and immunomodulatory), is one of the most important proteins present in mammalian milk. Protection against gastroenteritis is the most likely biologically relevant activity of lactoferrin. Multiple in vitro and animal studies have shown a protective effect of lactoferrin on infections with enteric microorganisms, including rotavirus, Giardia, Shigella, Salmonella and the diarrheagenic Escherichia coli. Lactoferrin has two major effects on enteric pathogens: it inhibits growth and it impairs function of surface expressed virulence factors thereby decreasing their ability to adhere or to invade mammalian cells. Thus, lactoferrin may protect infants from gastrointestinal infection by preventing the attachment by enteropathogens in the gut. Recently several clinical trials in children have started to address this issue. Whether lactoferrin can prevent a significant portion of diarrheal disease remains to be determined.

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Free secretory component and lactoferrin of human milk inhibit the adhesion of enterotoxigenic Escherichia coli

Cited by 109 publications

References 43 publications

Inhibition of enterotoxigenic Escherichia coli (ETEC) adhesion to Caco-2 cells by human milk and its immunoglobulin and non-immunoglobulin fractions

Inhibition of enterotoxigenic Escherichia coli (ETEC) adhesion to Caco-2 cells by human milk and its immunoglobulin and non-immunoglobulin fractions

IL-8 Released Constitutively by Primary Bronchial Epithelial Cells in Culture Forms an Inactive Complex with Secretory Component

Effect of lactoferrin on enteric pathogens

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