Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection

Superti, Fabiana; Siciliano, Rosa Anna; Rega, Barbara; Giansanti, Francesco; Valenti, Piera; Antonini, Giovanni

doi:10.1016/s0304-4165(01)00178-7

Cited by 97 publications

(83 citation statements)

References 40 publications

(57 reference statements)

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“…At these pH values the LF net charge is +23e, +14e and +4e. Titration simulations estimate pI to 9.4, slightly above the experimental range, 8-9 [17,18,19]. At pH 5 the interaction is purely repulsive due to a large net charge of the proteins.…”

Section: Mainmentioning

confidence: 79%

Molecular evidence of stereo-specific lactoferrin dimers in solution

Persson

Lund

Forsman

et al. 2010

Biophysical Chemistry

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Section: Mainmentioning

confidence: 79%

Molecular evidence of stereo-specific lactoferrin dimers in solution

Persson

Lund

Forsman

et al. 2010

Biophysical Chemistry

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“…Multiple studies have shown that apo-lactoferrin (iron-depleted lactoferrin) and hololactoferrin (iron-saturated lactoferrin) from bovine milk suppress rotavirus attachment and replication in vitro [12][13][14]; however, not all investigators have been able to confirm an effect [15]. The effect of lactoferrin on other viral enteritis organisms has not been fully evaluated.…”

Section: Effect Of Lactoferrin On Enteric Virusesmentioning

confidence: 99%

Effect of lactoferrin on enteric pathogens

Ochoa

Cleary²

2009

Biochimie

113

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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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“…32,33 Briefly, bLf was dissolved in 50 mM ammonium bicarbonate, pH 8.5, and trypsin (from bovine pancreas TPCK-treated, Sigma Chemical Company, St.Louis, MO, USA) digestion was performed at 37uC overnight using an enzyme to substrate ratio of 1 : 50 w/w. The N-and C-lobes obtained by enzymatic hydrolysis were purified by RP-HPLC chromatography and analysed by SDS-PAGE and mass spectrometry to check identity and purity.…”

mentioning

confidence: 99%

Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus

Ammendolia¹,

Agamennone

Pietrantoni³

et al. 2012

Pathogens and Global Health

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Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C-and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA 2 region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.

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Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection

Cited by 97 publications

References 40 publications

Molecular evidence of stereo-specific lactoferrin dimers in solution

Molecular evidence of stereo-specific lactoferrin dimers in solution

Effect of lactoferrin on enteric pathogens

Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus

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