Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

Rahman, Morshedur; Kim, Woan-Sub; Kumura, Haruto; Shimazaki, K.

doi:10.1007/s10529-009-9936-1

Cited by 11 publications

(11 citation statements)

References 30 publications

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“…Bovine C-lobe was demonstrated to promote bifidobacterial growth despite the fact that it did not bind with surface proteins from bifidobacteria, unlike the N-lobe and native lactoferrin which showed binding to those proteins, indicating that C-lobe may be enhancing bifidobacterial growth using mechanisms other than direct binding with the surface proteins from bifidobacteria [27, 28]. …”

Section: Therapeutic Applications Of C-lobementioning

confidence: 99%

C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule

Sharma

Sinha

Kaushik

et al. 2013

Biochemistry Research International

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Lactoferrin is an iron-binding diferric glycoprotein present in most of the exocrine secretions. The major role of lactoferrin, which is found abundantly in colostrum, is antimicrobial action for the defense of mammary gland and the neonates. Lactoferrin consists of two equal halves, designated as N-lobe and C-lobe, each of which contains one iron-binding site. While the N-lobe of lactoferrin has been extensively studied and is known for its enhanced antimicrobial effect, the C-lobe of lactoferrin mediates various therapeutic functions which are still being discovered. The potential of the C-lobe in the treatment of gastropathy, diabetes, and corneal wounds and injuries has been indicated. This review provides the details of the proteolytic preparation of C-lobe, and interspecies comparisons of its sequence and structure, as well as the scope of its therapeutic applications.

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Section: Therapeutic Applications Of C-lobementioning

confidence: 99%

C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule

Sharma

Sinha

Kaushik

et al. 2013

Biochemistry Research International

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“…Although the mechanism underlying the iron uptake of bifidobacteria is not clear at present, Lf-binding protein in several Bifidobacterium spp. has been reported (Kim et al, 2002Rahman et al, 2008Rahman et al, , 2009a and alteration of bLf iron content did not affect the binding ability (Rahman et al, 2009b). However, the mechanism of interaction between Lf and bifidobacteria is yet to be resolved.…”

Section: Resultsmentioning

confidence: 83%

“…, 2002, 2004; Rahman et al. , 2008, 2009a,b) and alteration of bLf iron content did not affect the binding ability (Rahman et al. , 2009b).…”

Section: Resultsmentioning

confidence: 99%

Screening of Bifidobacterium spp. based on in vitro growth responses to bovine lactoferrin

Rahman

Kim

Kumura

et al. 2010

Int J of Food Sci Tech

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In the present study, we investigated the in vitro growth responses of fourteen strains of four Bifidobacterium spp. (Bifidobacterium infantis, B. breve, B. bifidum, B. longum) against bovine lactoferrin (bLf) at various concentrations. Bacterial strains were grown in deMan, Rogosa and Sharpe (MRS) broth with or without bLf, and growth was monitored by measuring absorbance at 660 nm. A dose-dependent and straindependent growth response was observed. Bifidobacterium spp. were ranked into high, medium and low according to their calculated relative growth response levels against lactoferrin (Lf). Strains showed better growth responses against holo-type Lf. However, no inhibitory effects at high concentrations (4 mg mL )1 ) or with apo-type Lf were observed. These results strongly suggest that the growth response of Bifidobacterium spp. against bLf may be a selection criterion for their use in fermented products. In addition, use of holo-type Lf in fermented food products may be more effective for probiotic growth, and could also be used as a source of iron to the host.

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“…Structure and sequence analysis indicate that the two lobes might have arisen by gene duplication in the process of evolution (Lambert et al 2005). Separation of the N-lobe and Clobe is necessary for studying the structure-function relationship of LF (Rahman et al 2009), but it is difficult to achieve in native LF by proteolysis or chemical cleavage (Shimazaki et al 1993;Brines and Brock 1983). Several expression systems including bacteria, yeast, fungi, insect and mammary bioreactor are used to study recombinant mammalian proteins, especially Escherichia coli (E.coli) and Pichia pastoris systems.…”

Section: Introductionmentioning

confidence: 99%

Cloning, expression and characterization of Kunming mice lactoferrin and its N-lobe

Wang¹,

Tian²,

Teng³

et al. 2010

Biometals

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The lactoferrin cDNA of Kunming mice was isolated by reverse transcription polymerase chain reaction and cloned into vector pET28a(+). Its deduced amino acid sequence was analyzed and compared with lactoferrin of other species. Its secondary and tertiary structure are predicted and modeled by bioinformatics tools online. Then recombinant Kunming mice lactoferrin and its N-lobe were both expressed successfully in the Escherichia coli BL21(DE3) in the form of inclusion bodies. After purification with Ni-NTA His-Bind resin, the yield of recombinant lactoferrin was 17 mg l(-1) with purity of 92.1%, and that of lactoferrin N-lobe was 20 mg l(-1) with purity of 98.5%. The inhibition efficiency of refolded lactoferrin N-lobe against Staphylococcus aureus ATCC 25923 reaches 48.6% at the concentration of 25 micromol l(-1). However, the refolded lactoferrin (12.5 micromol l(-1)) didn't display obvious inhibition activity in the test. The expression of recombinant Kunming mice lactoferrin and its N-lobe will be helpful for the study of lactoferrin on structure, function and application in a mouse model system.

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Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

Cited by 11 publications

References 30 publications

C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule

C-Lobe of Lactoferrin: The Whole Story of the Half-Molecule

Screening of Bifidobacterium spp. based on in vitro growth responses to bovine lactoferrin

Cloning, expression and characterization of Kunming mice lactoferrin and its N-lobe

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