Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin

Kaminogawa, Shuichi; Shimizu, Makoto; Ametani, Akio; Hattori, Makoto; Ando, Osamu; Hachimura, Satoshi; Nakamura, Yuka; Totsuka, Mamoru; Yamauchi, Kunio

doi:10.1016/0167-4838(89)90117-9

Cited by 83 publications

(86 citation statements)

References 21 publications

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“…This assumption was tested using an allergen in milk, ␤-lactoglobulin (BLG). BLG contains two disulfides (19) that, when disrupted by site-directed mutagenesis, changed its structure (20) and the accessibility of IgGand IgE-binding epitopes (21,22). The disruption of disulfide bonds in BLG also had an impact on the sensitivity of this protein to digestion with pepsin and its overall allergenicity with respect to skin test responses and GI symptoms in a sensitized dog model of food allergy (12).…”

Section: Discussionmentioning

confidence: 99%

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Sen¹,

Kopper²,

Pons³

et al. 2002

The Journal of Immunology

208

191

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Hypersensitivity to peanuts is a reaction mediated by IgE Abs in response to several peanut protein allergens. Among these allergenic proteins, Ara h 2 is one of the most commonly recognized allergens. Ara h 2 is a 17-kDa protein that has eight cysteine residues that could form up to four disulfide bonds. Circular dichroism studies showed substantial changes in the secondary and tertiary structures of the reduced Ara h 2 as compared with the native protein. Upon treatment with trypsin, chymotrypsin, or pepsin, a number of relatively large fragments are produced that are resistant to further enzymatic digestion. These resistant Ara h 2 peptide fragments contain intact IgE-binding epitopes and several potential enzyme cut sites that are protected from the enzymes by the compact structure of the protein. The enzyme-treated allergen remains essentially intact despite the action of proteases until the fragments are dissociated when the disulfide linkages are reduced. Amino acid sequence analysis of the resistant protein fragments indicates that they contain most of the immunodominant IgE-binding eptiopes. These results provide a link between allergen structure and the immunodominant IgE-binding epitopes within a population of food-allergic individuals.

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Section: Discussionmentioning

confidence: 99%

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Sen¹,

Kopper²,

Pons³

et al. 2002

The Journal of Immunology

208

191

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show abstract

“…␤-LG is a predominant whey protein of 18 kDa with two disulfide bridges, as well as free cysteine (McKenzie, 1971). Many physicochemical and physiological studies on this protein have been carried out: its higher ordered structure (Townend et al, 1967;Papiz et al, 1986;Gu & Brady, 1992;Papiz et al, 1986;Brownlow et al, 1997;Kuwata et al, 1999), unfolding (Alexander & Pace, 1971;Sawyer et al, 1971, Kaminogawa et al, 1989Laligant et al, 1994;Dufour et al, 1994;Katou et al, 2001), refolding (Hattori et al, 1993;Creamer, 1995;Hamada et al, 1996;Ragona et al, 1999;Forge et al, 2000;Kuwata et al, 2001), polymerization and gelation behavior (Mulvihill & Kinsella, 1987;Laligant et al, 1991;Foegeding et al, 1992), foaming and emulsifying properties (Shimizu et al, 1985;Waniska & Kinsella, 1988), immunological response (Kurisaki et al, 1982;Kurisaki et al, 1985;Takahashi et al, 1988;Takahashi et al, 1990;Tsuji et al, 1993;Totsuka et al, 1997;Mantyjarvi et al, 2000) and so on. This protein consists of nine antiparallel ␤-sheets and one ␣-helix to form a calyx shaped ␤-barrel structure, and it is categorized as a member of the lipocalin superfamily (Flower, 1996;Sawyer & Kontopidis, 2000).…”

Section: Designing Of Functional Improvements In Food Proteins In Mulmentioning

confidence: 99%

“…We also explored the conformation of the conjugates by four methods: retinol-binding activity measurement, CD spectra, intrinsic fluorescence and ELISA with monoclonal antibodies (mAbs) (Kaminogawa et al, 1987;1989;Hattori et al, 1993). Retinol-binding activity of each conjugate was similar to that of ␤-LG.…”

Section: Functional Changes In ␤-Lg By Conjugation With Cmd Of 10 Kdamentioning

confidence: 99%

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Hattori

2002

FSTR

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Many studies on the conjugates of proteins and saccharides (neoglycoproteins) have been carried out over the past 20 years to improve the function of proteins. However, most have been carried out by attachment or elimination of low-molecular weight molecules for single purposes. The structure-function relationship of the conjugates has not been well understood, and little is known about the improvement of proteins by conjugation with polysaccharides. We sought to achieve functional improvements in food proteins in multiple aspects by conjugation with charged polysaccharides. We chose bovine ␤-lactoglobulin (␤-LG) as the target protein for improvement of the function and attached carboxymethyl dextrans (CMDs) of different molecular weight (10, 40, 70 and 162 kDa) covalently. After conjugation and purification, we explored the structure of the ␤-LG-CMD conjugates to prove that we could prepare conjugates while maintaining the native-like structure of protein molecule. By conjugation with CMDs, enhancement of thermal stability, improvement in the emulsifying properties and reduction of immunogenicity of ␤-LG could be achieved. Increases in the CMD content and net charge were viewed as the major factors in the improved emulsifying properties. Conjugation with high saccharide content using polysaccharides of higher molecular weight is believed to be effective in reduced immunogenicity of ␤-LG.

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“…The production of monoclonal antibodies (mAbs) is an appropriate and well-used strategy for stably and precisely assessing the denaturation state of a protein. MAbs specific to some thermally denatured states of -lactoglobulin 6) or ovalbumin 7) have therefore been produced. Hen's egg is the most frequent cause of food allergy, and approximately two-thirds of children diagnosed with food allergy are reactive to egg white.…”

mentioning

confidence: 99%

Recognition of Native and/or Thermally Induced Denatured Forms of the Major Food Allergen, Ovomucoid, by Human IgE and Mouse Monoclonal IgG Antibodies

Hirose

Kitabatake

Kimura³

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin

Cited by 83 publications

References 21 publications

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Protein Structure Plays a Critical Role in Peanut Allergen Stability and May Determine Immunodominant IgE-Binding Epitopes

Functional Improvements in Food Proteins in Multiple Aspects by Conjugation with Saccharides: Case Studies of .BETA.-Lactoglobulin-Acidic Polysaccharides Conjugates.

Recognition of Native and/or Thermally Induced Denatured Forms of the Major Food Allergen, Ovomucoid, by Human IgE and Mouse Monoclonal IgG Antibodies

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