Bovine lactoferrin digested with human gastrointestinal enzymes inhibits replication of human echovirus 5 in cell culture

Furlund, Camilla B.; Kristoffersen, Anja Bråthen; Devold, Tove Gulbrandsen; Vegarud, Gerd Elisabeth; Jonassen, Christine Monceyron

doi:10.1016/j.nutres.2012.06.006

Cited by 23 publications

(16 citation statements)

References 62 publications

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“…A two-phase digestion procedure was performed according to the method described by Furlund et al [29]. Gastric and intestinal digestion phases were performed at 37 °C, in a shaking bath (180 rpm/min).…”

Section: In Vitro Digestion Processmentioning

confidence: 99%

Phenolic composition, antioxidant capacity, energy content and gastrointestinal stability of Croatian wild edible plants

Poljuha

Šola

Bilić³

et al. 2015

Eur Food Res Technol

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broom 40 % ethanolic extract. Phenolic acids of the three species were not stable during gastric and duodenal phases of simulated digestion. Two main black bryony kaempferol glycosides were best preserved after digestion (50 % of each). Black bryony contains more energy than wild asparagus and butcher's broom. Accordingly, we propose black bryony as a valuable source of antioxidant kaempferol glycosides with relevant gastrointestinal stability and higher energy content than so far more conventional vegetable wild asparagus.

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Section: In Vitro Digestion Processmentioning

confidence: 99%

Phenolic composition, antioxidant capacity, energy content and gastrointestinal stability of Croatian wild edible plants

Poljuha

Šola

Bilić³

et al. 2015

Eur Food Res Technol

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“…Cationic peptide-or proteinbased delivery systems are soluble in water, but their susceptibility to peptic digestion in the stomach may result in the loss of protection before absorption occurs. 21 These disadvantages necessitate the development of a water-soluble, pepsin-resistant, cationic delivery system. β-Lactoglobulin (BLG), a 162-residue globular protein, makes up approximately 60% of bovine whey protein.…”

Section: ■ Introductionmentioning

confidence: 99%

Cationic β-Lactoglobulin Nanoparticles as a Bioavailability Enhancer: Protein Characterization and Particle Formation

et al. 2013

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Cationic β-lactoglobulin (CBLG) was developed as a bioavailability enhancer for poorly absorbed bioactives. At most 11 anionic amino acid residues of β-lactoglobulin (BLG) were substituted by ethylenediamine (EDA), resulting in a highly positive surface charge (zeta potential up to 39 mV at pH 7.0) and significantly increased surface hydrophobicity. These changes conferred CBLG with desirable water solubility and improved mucoadhesion by at most 252%, according to quartz crystal microbalance (QCM) study. Furthermore, CBLG inherited the unique resistance to gastric digestion from BLG, while the digestion under simulated intestinal condition was significantly improved. The latter was possibly due to the formation of aspartic acid-EDA conjugates, together with the randomization of protein conformation related with decreased percentage of β-sheet. Compared to BLG, CBLG formed smaller (75-94 nm), more uniform nanoparticles by the acetone-desolvation method. These merits made CBLG a useful material that provides desirable solubility, controlled release, and enhanced absorption to nutraceuticals or drugs.

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“…Bovinelactoferrin and lactoferrin inhibits viral binding, exhibits cytopathic effect and antigen synthesis,inhibits viral replication prior to, during and subsequent to the viral adsorption step (Pietrantoni et al 2006;Furlund et al 2012) Enterovirus Porcine lactoferrin blocks the adsorption or receptor-mediated binding of the virus to the target cell membrane (Chen et al 2008) Poliovirus Bovine lactoferrin targets viral adsorption, binds to the surfaces of host cells and prevents attachment of virus particles, competes for viral receptor interaction (McCann et al 2003;Marchetti et al 1999) Human rotavirus…”

Section: Resultsmentioning

confidence: 99%

Antiviral activities of whey proteins

Cheung

Wong

et al. 2015

Appl Microbiol Biotechnol

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Milk contains an array of proteins with useful bioactivities. Many milk proteins encompassing native or chemically modified casein, lactoferrin, alpha-lactalbumin, and beta-lactoglobulin demonstrated antiviral activities. Casein and alpha-lactalbumin gained anti-HIV activity after modification with 3-hydroxyphthalic anhydride. Many milk proteins inhibited HIV reverse transcriptase. Bovine glycolactin, angiogenin-1, lactogenin, casein, alpha-lactalbumin, beta-lactoglobulin, bovine lactoferrampin, and human lactoferrampin inhibited HIV-1 protease and integrase. Several mammalian lactoferrins prevented hepatitis C infection. Lactoferrin, methylated alpha-lactalbumin and methylated beta-lactoglobulin inhibited human cytomegalovirus. Chemically modified alpha-lactalbumin, beta-lactoglobulin and lysozyme, lactoferrin and lactoferricin, methylated alpha-lactalbumin, methylated and ethylated beta-lactoglobulins inhibited HSV. Chemically modified bovine beta-lactoglobulin had antihuman papillomavirus activity. Beta-lactoglobulin, lactoferrin, esterified beta-lactoglobulin, and esterified lactoferrindisplayed anti-avian influenza A (H5N1) activity. Lactoferrin inhibited respiratory syncytial virus, hepatitis B virus, adenovirus, poliovirus, hantavirus, sindbis virus, semliki forest virus, echovirus, and enterovirus. Milk mucin, apolactoferrin, Fe(3+)-lactoferrin, beta-lactoglobulin, human lactadherin, bovine IgG, and bovine kappa-casein demonstrated antihuman rotavirus activity.

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Bovine lactoferrin digested with human gastrointestinal enzymes inhibits replication of human echovirus 5 in cell culture

Cited by 23 publications

References 62 publications

Phenolic composition, antioxidant capacity, energy content and gastrointestinal stability of Croatian wild edible plants

Phenolic composition, antioxidant capacity, energy content and gastrointestinal stability of Croatian wild edible plants

Cationic β-Lactoglobulin Nanoparticles as a Bioavailability Enhancer: Protein Characterization and Particle Formation

Antiviral activities of whey proteins

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