Lactoferrin: A Marvelous Protein in Milk

Shimazaki, K.

doi:10.2508/chikusan.71.329

Cited by 45 publications

(54 citation statements)

References 108 publications

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“…The concentrations of lactoferrin range from 0AE02 to 0AE2 mg ml )1 in bovine milk to 2 mg ml )1 in human milk (Shimazaki 2000). In addition, Bellamy et al (1992) isolated and sequenced the antibacterial peptides, lactoferricin H from a digest of human lactoferrin (residues 1-47) and lactoferricin B from a digest of bovine lactoferrin (residues 17-41), with both peptides being derived from the N-terminal domain of the respective lactoferrin molecules.…”

Section: Introductionmentioning

confidence: 99%

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

et al. 2003

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Aims:To characterize the effect of bovine lactoferrin and lactoferricin B against feline calicivirus (FCV), a norovirus surrogate and poliovirus (PV), as models for enteric viruses. Methods and Results: Crandell-Reese feline kidney (CRFK) cells were used for the propagation of FCV and monkey embryo kidney (MEK) cells for PV. The assays included visual assessment of cell lines for cytopathic effects and determination of the percentage cell death using MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium] dye reduction assay. Incubation of bovine lactoferrin with CRFK cells either prior to or together with FCV inoculation substantially reduced FCV infection. In contrast, the interference of lactoferrin with the infection of cells with PV was demonstrated only when lactoferrin was present with cell lines and virus for the entire assay period. Using indirect immunofluorescence, lactoferrin was detected on the surface of both CRFK and MEK cells, suggesting that the interference of viral infection may be attributed to lactoferrin binding to the surfaces of susceptible cells, thereby preventing the attachment of the virus particles. Lactoferricin B, a cationic antimicrobial peptide derived from the N-terminal domain of bovine lactoferrin, reduced FCV but not PV infection. Conclusion: Lactoferrin was shown to interfere with the infection of cells for both FCV and PV. However, lactoferricin B showed no interference of infection with PV and interference with infection for FCV required the presence of lactoferricin B together with the cell line and virus. Significance and Impact of the Study: An in vitro basis is provided for the effects of bovine lactoferrin and lactoferricin B in moderating food-borne infections of enteric viruses.

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Section: Introductionmentioning

confidence: 99%

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

et al. 2003

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“…tears, saliva etc. and is also found in the granules of the neutrophils as reviewed by Shimazaki [1]. This 80 kDa protein is composed of a single polypeptide chain of about 690 amino acid residues and is folded into two homologous (~ 40% sequence identity) lobes, representing its N-and C-terminal halves and connected by a short "hinge" peptide of 10-15 residues.…”

Section: Introductionmentioning

confidence: 99%

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

et al. 2009

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Bovine lactoferrin (bLf) is a multifunctional iron-binding glycoprotein secreted mainly in milk and other secretory fluids. Bovine lactoferrin is reported to promote the growth of bifidobacteria and binding of bLf to bifidobacteria cell is thought to be involved. After separation of bLf half molecule and extraction of surface proteins from bifidobacteria, binding profiles were observed by immunoblotting. No binding was appeared when bLf C-lobe was being reacted with cell surface proteins on PVDF membrane. Conversely, a 50-kDa band was appeared when reacted with either intact bLf or nicked bLf. This result strongly suggests that binding region could be N-lobe.Moreover, blot, probed with nicked bLf, reacted with anti-lactoferricin antibody also produced a 50-kDa band that indicates the binding occurred at lactoferricin region of bLf molecule. Interestingly, despite absence of binding, bLf C-lobe can stimulate the growth of bifidobacteria.

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“…Ademais, segundo Shimazaki (2000), a sua funcionalidade como agente antimicrobiano torna-se reduzida na presença de cátions divalentes, como cálcio e magnésio, encontrados em vários alimentos.…”

Section: Introductionunclassified

Análise Da Cor E Da Atividade Antimicrobiana De Microcápsulas Contendo Lactoferrina Bovina

2014

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Lactoferrina bovina (bLF), proveniente do soro de leite, foimicroencapsulada pela técnica de spray drying. Microcápsulascontendo 20 % de bLF foram produzidas, utilizando-se comomaterial de parede dextrina: amido octenilsuccinato (OSA) emdiferentes proporções: 100:00, 75:25, 50:50, 25:75 e 0:100 %.Foram avaliadas a cor e a estabilidade de cor das microcápsulassob armazenamento em ambientes com diferentes umidadesrelativas e a atividade antimicrobiana da lactoferrina liberadadas microcápsulas. As microcápsulas apresentaram cor clara etenderam a escurecer sob armazenamento em ambiente com altaumidade relativa. Verifi cou-se atividade inibitória das microcápsulasde bLF produzidas para diferentes bactérias Gram positivas(Bacillus subtilis CCT 2576, Staphylococcus aureus CCT 2740,Micrococcus luteus CCT 2692, Enterococcus faecium CCT 5079,Streptococcus faecium ATCC 10541, Rhodococcus equi CCT0541), Gram negativas (Pseudomonas aeruginosa ATCC 13388,Salmonella choleraesius CCT 4296, Escherichia coli CCT 0547) elevedura (Candida albicans ATCC 10231). A concentração inibitóriamínima (MIC) das microcápsulas variou de acordo com o microorganismotestado (MIC entre 2,5-100 mg.mL-1). Com exceção deB. subtilis (MIC entre 50-100 mg.mL-1 para as microcápsulas), aconcentração de bLF contida nas microcápsulas necessária parainibir o crescimento dos micro-organismos foi menor do que a bLFnativa. Esses resultados sugerem efeito de potencialização daatividade antimicrobiana da bLF após o processamento por spraydrying.

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Lactoferrin: A Marvelous Protein in Milk

Cited by 45 publications

References 108 publications

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

Análise Da Cor E Da Atividade Antimicrobiana De Microcápsulas Contendo Lactoferrina Bovina

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